Engineered cells for production of phenyl acetate

Abstract

Described in this application are host cells comprising heterologous polynucleotides encoding a 4-hydroxybenzoate decarboxylase (4-HB DC) and / or an acetyl transferase, as well as methods of culturing the host cells. Also described are methods of producing a product of interest, such as phenyl acetate or phenol, using the host cells described herein.

Description

[0001] ENGINEERED CELLS FOR PRODUCTION OF PHENYL ACETATE FIELD The present disclosure relates to production of phenyl acetate in a host cell. RELATED APPLICATIONS This application claims the benefit under 35 U.S.C. § 119(e) of U.S. Provisional Application No.63 / 682,993, filed August 14, 2024, the entire content of which is hereby incorporated by reference in its entirety. REFERENCE TO AN ELECTRONIC SEQUENCE LISTING The contents of the electronic sequence listing (G091970123WO00-SEQ-CRP.xml; Size: 82,175 bytes; and Date of Creation: August 12, 2025) are herein incorporated by reference in its entirety. BACKGROUND Phenol is useful for several industrial processes, such as the production of phenolic resins, the manufacture of synthetic fibers, and the production of slimicides, herbicides, disinfectants, antiseptics, and medicinal preparations (e.g., mouthwash and sore throat lozenges). Production of phenol is challenging because of phenol’s toxicity. Phenyl acetate, a variant of phenol, is less toxic, and is also useful as a solvent. SUMMARY Aspects of the present disclosure relate, at least in part, to a host cell that comprises a heterologous polynucleotide encoding an acetyl transferase (AcT), wherein the host cell is capable of converting phenol to phenyl acetate (phenylacetate or PA). Aspects of the present disclosure relate, at least in part, to a host cell that comprises a heterologous polynucleotide encoding a 4-hydroxybenzoate decarboxylase (4-HB DC or DC), wherein the host cell is capable of converting 4-hydroxybenzoate to phenol. In some embodiments, the host cell is not a bacterial cell. Aspects of the present disclosure relate, at least in part, to host cells comprising one or more heterologous polynucleotides collectively encoding: (i) a 4-hydroxybenzoate decarboxylase (4-HB DC); and (ii) an acetyl transferase (AcT), wherein the host cell is capable of converting hydroxybenzoate to phenol and converting phenol to phenyl acetate. In some embodiments, the host cell is a yeast cell. In some embodiments, the yeast cell is a Saccharomyces cell. In some embodiments, the Saccharomyces cell is Saccharomyces cerevisiae cell. In some embodiments, the host cell is a bacterial cell. In some embodiments the bacterial cell is an E. coli cell. In some embodiments, the host cell comprises a heterologous polynucleotide encoding an AcT, wherein the AcT comprises a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to any one of SEQ ID NOs: 1-6. In some embodiments, the AcT comprises the sequence of any one of SEQ ID NOs: 1-6. In some embodiments, the AcT is a benzoyl transferase. In some embodiments, the host cell comprises at least two, at least three, or at least four copies of a heterologous polynucleotide encoding AcT. In some embodiments, the host cell comprises one or more polynucleotides collectively encoding two or more of: an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 1; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 2; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 3; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 4; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 5; and an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 6. In some embodiments, the host cell comprises a heterologous polynucleotide encoding a 4-hydroxybenzoate decarboxylase (4-HB DC or DC), wherein the 4-HB DC comprises a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to any one of SEQ ID NOs: 14-16. In some embodiments, the 4-HB DC comprises the sequence of any one of SEQ ID NOs: 14-16. In some embodiments, each of SEQ ID NOs: 14-16 represents a different subunit of the 4-HB DC, and the 4-HB DC comprises all these subunits. In some embodiments, the host cell comprises at least two, at least three, or at least four copies of a heterologous polynucleotide encoding 4-HB DC. In some embodiments, the host cell comprises one or more polynucleotides collectively encoding two or more of: a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID No: 14; a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 15; and a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 16. In some embodiments, the host cell comprises at least one heterologous polynucleotide encoding a 4-hydroxybenzoate decarboxylase (4-HB DC), wherein the 4-HB DC comprises a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to any one of SEQ ID NOs: 14-16; and at least one heterologous polynucleotide encoding an acetyl transferase (AcT), wherein the AcT comprises a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to any one of SEQ ID NOs: 1-6. In some embodiments, the host cell comprises one or more polynucleotides collectively encoding: a) two or more of: a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NOs: 14; a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NOs: 15 a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 16; and b) two or more of: an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 1; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 2; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 3; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 4; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 5; and an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 6. In some embodiments, the host cell comprises one or more genetic modifications that result in decreased expression, relative to a control host cell lacking the one or more genetic modifications, of at least one endogenous gene encoding an esterase. In some embodiments, the host cell has decreased expression of one or more of SAY1 and / or IAH1, relative to a control host cell lacking a decrease in expression of one or more of SAY1 and / or IAH1. In some embodiments, the one or more genetic modifications comprise a knockout of an endogenous gene encoding an esterase. In some embodiments, the one or more genetic modifications comprise: a knockout of SAY1 and / or a knockout of IAH1. In some embodiments, the host cell produces more phenyl acetate compared to a control host cell that does not comprise the one or more genetic modifications that result in decreased expression of at least one endogenous gene encoding an esterase. Aspects of the disclosure provide, at least in part, methods for producing phenyl acetate, the method comprising culturing a host cell associated with the disclosure. In some embodiments, the method further comprises isolating phenyl acetate from the cell culture. In some embodiments, the cell is cultured at pH of about 6 or below. BRIEF DESCRIPTION OF DRAWINGS The accompanying drawings are not intended to be drawn to scale. The drawings are illustrative only and are not required for enablement of the disclosure. For purposes of clarity, not every component may be labeled in every drawing. In the drawings: FIGs.1A-1B are diagrams illustrating a biosynthetic pathway for the bioproduction of phenol and phenyl acetate including the enzymatic conversion of 4-hydroxybenzoate to phenol and phenyl acetate (FIG.1A); and the bioconversion of glucose (via multiple steps) to 4- hydroxybenzoate, phenol and phenylacetate (FIG.1B), where TKL is transketolase, TAL is transaldolase, PPP is Pentose phosphate pathway, DAHP synthase, aroG / F / H is DAHP synthase, aroB is DHQ synthase, aroD is DH-quinase, aroE is shikimate dehydrogenase, aroK is shikimate kinase, aroA is 5-enolpyruvylshikimate-3-phosphate synthase, aroC is chorismate synthase, and CPL is chorismate lyase. Note that some substrates, products, intermediates, enzymes, etc. involved in this pathway may be omitted from this diagram. FIG.1C is a diagram showing an alternative biosynthetic pathway bioproduction of phenol acetate including: the enzymatic conversion of 4-HB to 4-acetoxybenzoate, and the enzymatic conversion of 4-acetoxybenzoate to phenyl acetate. FIG.2 illustrates abundances of 4-hydroxybenzoate (4-HB) and phenol (representing the conversion from 4-HB to phenol) in host cells expressing exemplary 4-HB decarboxylases. FIG.3 illustrates the abundance of phenyl acetate (PA) (representing the conversion of phenol to phenyl acetate) in host cells expressing exemplary acetyl transferases. FIG.4 illustrates the abundance of phenyl acetate (PA) (representing the conversion of 4-HB to phenyl acetate via a two-step reaction involving decarboxylation and acetylation) in host cells expressing exemplary 4-HB decarboxylases and acetyl transferases. DETAILED DESCRIPTION Phenol is a common solvent, used, for example, in production of synthetic fibers, such as nylon. Production of phenol by conventional means (e.g., cumene peroxidation, Schmidt 2005 App. Catal. A: General 280: 89) is very energy intensive and produces a large amount of toxic waste (Wierckx et al.2005 App. Env. Mic.71: 8221). Bioproduction of phenol is a desirable alternative. However, phenol is highly toxic to cells, which is challenging for large scale bioproduction. This disclosure is based in part on the engineering of an enzymatic pathway for producing phenyl acetate (also known as “phenylacetate”) from 4-hydroxybenzoate (4-HB). Phenyl acetate is less toxic than phenol, which allows for large-scale bioproduction. Phenyl acetate may be converted to phenol once it has been isolated from cells, as described herein and in art. Alternatively, phenyl acetate itself is also useful as a solvent or product, or an intermediate in production of medicines, pesticides and other industrial useful chemicals (CN109574831B, CN109534995B, KR100422883B1, CS146999B1, CN109534995B, and WO2023140793A2). 1. Biosynthesis of Phenyl Acetate and Phenol FIGs.1A-1B show a phenol and phenyl acetate biosynthesis pathway. Phenol and phenylacetate (PA) can be produced from 4-hydroxybenzoate (4-HB) by enzymatic conversion using a decarboxylase and an acetyltransferase. For example, 4-hydroxybenzoate (4-HB) can be converted to phenol by a decarboxylase (DC) enzyme (FIG.1A). In a second step, phenol can be converted to phenyl acetate by an acetyltransferase (AcT) enzyme (FIG.1A). FIG.1B illustrates a pathway in which phenyl acetate can be generated from glucose through the shikimate pathway, which includes the intermediate chorismate, a precursor to 4- hydroxybenzoate. Examples of shikimate pathway enzymes that can be used to produce phenol and phenylacetate include: 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase (DAHP synthase, or aroG / F / H according to E. coli nomenclature, EC 4.1.2.15), which catalyzes the condensation of (a) phosphoenol pyruvate (PEP) and (b) erythrose-4-phosphate (E4P) to synthesize 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP); 3-dehydroquinate synthase (DHQ synthase, aroB, EC 4.6.1.3), which converts DAHP to 3-dehydroquinate (DHQ); 3- dehydroquinate dehydratase (DH-quinase, aroD, EC 4.2.1.10), which converts DHQ to 3- dehydroshikimate (DHS); shikimate dehydrogenase (Shikimate_DH, aroE, EC 1.1.1.25), which synthesizes shikimate from DHS; shikimate kinase (SKI, aroK, EC 2.7.1.71), which converts shikimate to shikimate-3-phosphate; and 5-enolpyruvylshikimate-3-phosphate synthase (EPSP, aroA, EC 2.5.1.19), which converts shikimate-3-phosphate to 5-enolpyruvylshikimate-3- phosphate (EPSP); and chorismate synthase (aroC, EC 4.6.1.4), which converts EPSP to chorismate. Chorismate can be converted to 4-hydroxybenzoate by chorismate lyase (CPL) as illustrated in FIG.1B. It is noted that some substrates, products, intermediates, enzymes, etc. involved in this pathway may be omitted from FIG.1B; one of ordinary skill in the art would be familiar with the various components and possible substitutions useful in this pathway, which are described in the art. PEP can be derived from glucose through glycolysis and its associated glycolytic enzymes, and E4P can be derived from glucose through the pentose phosphate pathway (PPP) and its associated PPP enzymes. The glycolytic enzymes useful for producing PEP are known to those in the art and include hexokinase, glucose-6-phosphate isomerase, phosphofructokinase, fructose-bisphosphate aldolase, triosephosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, phosphoglycerate mutase and phosphopyruvate hydratase (enolase). The PPP enzymes useful for producing E4P are known to those in the art and include glucose-6-phosphate dehydrogenase, gluconolactonase, 6-phosphogluconate dehydrogenase, ribulose-5-phosphate isomerase, ribulose-5-phosphate3-epimerase, transketolase (TKL) and transaldolase (TAL) (FIG.1B). Exemplary amino acid and nucleotide sequences of these enzymes are provided in Table 4. In some embodiments, the present disclosure pertains to a method of producing phenyl acetate as diagrammed in FIGS.1A and 1B. An alternative, inferior, method of production of phenyl acetate is diagrammed in FIG. 1C. This route for production of phenyl acetate (PA) from 4-hydroxybenzoate (4-HB) comprises these steps: Step (1): Acylating 4-HB to 4-Acetoxybenzoate, which could potentially be achieved with an acyltransferase, such as MsAcT, which is Mycobacterium smegmatis acyltransferase, which was described in Jost et al.2020 ACS Catal.10: 10500. Other enzymes that could potentially perform this step are widely known. Step (2): Subjecting the 4- acetoxybenzoate to a decarboxylation step, for example, with a decarboxylase (e.g., using any of various widely-known enzymes) to produce phenyl acetate. Applicants have discovered that this route (acylation followed by decarboxylation) does not work well in vivo, as 4-acetoxybenzoate is unstable and toxic. In some embodiments, a host cell comprising one or more proteins (or one or more heterologous polynucleotides encoding the one or more proteins) associated with the disclosure is capable of converting 4-hydroxybenzoate to phenol. In some embodiments, a host cell comprising one or more proteins (or one or more heterologous polynucleotides encoding the proteins) associated with the disclosure is capable of converting phenol to phenyl acetate. In some embodiments, a host cell comprising one or more proteins (or one or more heterologous polynucleotides encoding the proteins) associated with the disclosure is capable of converting 4- hydroxybenzoate to phenyl acetate. In some embodiments, a host cell comprising one or more proteins associated with the disclosure (e.g., a DC and / or an AcT) is capable of producing at least about 2 to 7 mg / L of phenyl acetate. In some embodiments, a host cell comprising one or more proteins (or one or more heterologous polynucleotides encoding the one or more proteins) associated with the disclosure may further include one or more additional copies of a polynucleotide encoding one or more enzymes useful for converting glucose to chorismate, for example, the enzymes in the shikimate pathway of FIG.1B and / or discussed herein for converting glucose to DAHP through glycolysis or the PPP pathway. Such a host cell may include five copies of a polynucleotide encoding aroF for example. 2. Polynucleotides Encoding an Acetyl Transferase (AcT) and / or a Decarboxylase (DC) Aspects of the present disclosure relate to polypeptides, functional modifications and variants thereof, polynucleotides encoding said polypeptides, as well as uses relating to any thereof. These polypeptides include variants of decarboxylases (DC) and / or variants of acetyl transferases (Act), such as DC variants capable of producing phenol from 4-HB and AcT variants capable of producing phenyl acetate from phenol. For example, the polypeptides and cells described in this application may be used to produce phenyl acetate, e.g., by converting 4- HB to phenol and converting phenol to phenyl acetate. The methods may comprise using a host cell comprising one or more enzymes disclosed in this application, a cell lysate, isolated enzymes, or any combination thereof. Methods comprising expression of polynucleotides encoding a polypeptide disclosed in this application in a host cell are encompassed by the present disclosure. In vitro methods comprising reacting one or more DCs and one or more AcTs in a reaction mixture disclosed in this application are also encompassed by the present disclosure. Decarboxylases Aspects of the present disclosure provide polynucleotides encoding decarboxylases (DC). As used herein, a “decarboxylase” refers to a polypeptide that has decarboxylase activity alone or in complex with another peptide. As used herein, “decarboxylase activity” refers to removing a carboxyl group from a substrate. A decarboxylase associated with the disclosure can use 4-hydroxybenzoate (4-HB) as a substrate. In some embodiments, a decarboxylase associated with the disclosure is a Klebsiella pneumoniae decarboxylase. In some embodiments, a decarboxylase comprises a complex of two or more polypeptides. In some embodiments, a decarboxylase comprises a complex of two or more of kpdD (Uniprot ID: Q462H2), kpdC (Uniprot ID: 462H3), and kpdB (Uniprot ID: Q462H4); these represent subunits of a DC, with sequences provided as SEQ ID NOs: 14, 15, and 16, respectively. In some embodiments, a decarboxylase comprises a complex of kpdD, kpdC, and kpdB. In some embodiments, a DC of the present disclosure comprises an amino acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, including all values in between, to the sequence of SEQ ID NO: 14. In some embodiments, a DC comprises the amino acid sequence of SEQ ID NO: 14. In some embodiments, a DC of the present disclosure comprises a sequence (e.g., amino acid sequence) that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 15. In some embodiments, a DC comprises the amino acid sequence of SEQ ID NO: 15. In some embodiments, a DC of the present disclosure comprises a sequence (e.g., amino acid sequence) that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 16. In some embodiments, a DC comprises the amino acid sequence of SEQ ID NO: 16. In some embodiments, a DC comprises a complex of two or more polypeptides (e.g., subunits), individually or collectively having decarboxylase activity. In some embodiments, a DC comprises a complex of 2, 3 or more polypeptides, each having and / or together having DC activity. In some embodiments, expression of one DC polypeptide in a host cell allows conversion of 4-HB to phenol. In some embodiments, expression of two DC polypeptides in a host cell enhances conversion of 4-HB to phenol. In some embodiments, expression of three DC polypeptides in a host cell enhances conversion of 4-HB to phenol. In some embodiments, a DC having decarboxylase activity comprises a complex of two or more of: (i) a polypeptide comprising a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 14; (ii) a polypeptide comprising a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 15; and (iii) a polypeptide comprising a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 16. In some embodiments, a DC comprises a complex of at least two polypeptides each comprising the amino acid sequence of any one of SEQ ID NOs: 14-16. In some embodiments, a DC having decarboxylase activity comprises a complex of each of: (i) a polypeptide comprising a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 14; (ii) a polypeptide comprising a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 15; and (iii) a polypeptide comprising a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 16. In some embodiments, a DC having decarboxylase activity comprises a complex of each of: (i) a polypeptide comprising the sequence of SEQ ID NO: 14, (ii) a polypeptide comprising the sequence of SEQ ID NO: 15, and (iii) a polypeptide comprising the sequence of SEQ ID NO: 16. In some embodiments, a DC described herein is encoded by a nucleic acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to any one of SEQ ID NOs: 17-22. In some embodiments, a DC described herein is encoded by the nucleic acid sequence of any one of SEQ ID NOs: 17-22. It should be appreciated that activity (e.g., specific activity) of a DC can be measured by any means known to one of ordinary skill in the art. In some embodiments, activity (e.g., specific activity) of a DC in a host cell may be measured as the concentration of 4-HB consumed or the concentration of phenol produced. In some embodiments, a polynucleotide encoding one or more of the DCs associated with the disclosure is integrated into the genome of a host cell. In other embodiments, one or more of the DCs associated with the disclosure is expressed on a plasmid in a host cell. Acetyl transferases Aspects of the present disclosure provide polynucleotides encoding acetyl transferases (AcT). As used herein, a “acetyl transferase” refers to an enzyme that transfers an acetyl group from one substrate to another. An AcT associated with the disclosure can use phenol as a substrate. In some embodiments, an AcT associated with the disclosure is a Saccharomyces cerevisiae AcT (strain ATCC 204508 / S288c). In some embodiments, an AcT associated with the disclosure is a Cucumis melo AcT (Benzyl alcohol O-benzoyltransferase-like, Uniprot accession number: P93094). In some embodiments, an AcT associated with the disclosure is a Lachancea mirantina AcT. In some embodiments, an AcT associated with the disclosure is a Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) AcT. In some embodiments, an AcT associated with the disclosure is a Saccharomyces eubayanus AcT. In some embodiments, an AcT is a benzoyl transferase. In some embodiments, an AcT of the present disclosure comprises an amino acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 1. In some embodiments, the AcT comprises the amino acid sequence of SEQ ID NO: 1. In some embodiments, an AcT of the present disclosure comprises an amino acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 2. In some embodiments, the AcT comprises the amino acid sequence of SEQ ID NO: 2. In some embodiments, an AcT of the present disclosure comprises an amino acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 3. In some embodiments, the AcT comprises the amino acid sequence of SEQ ID NO: 3. In some embodiments, an AcT of the present disclosure comprises an amino acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 4. In some embodiments, the AcT comprises the amino acid sequence of SEQ ID NO: 4. In some embodiments, an AcT of the present disclosure comprises an amino acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 5. In some embodiments, the AcT comprises the amino acid sequence of SEQ ID NO: 5. In some embodiments, an AcT of the present disclosure comprises an amino acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to the sequence of SEQ ID NO: 6. In some embodiments, the AcT comprises the amino acid sequence of SEQ ID NO: 6. In some embodiments, an AcT of the present disclosure is encoded by a sequence (e.g., nucleic acid sequence) that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to any one of SEQ ID NOs: 7-13. In some embodiments, an AcT of the present disclosure is encoded by the nucleic acid sequence of any one of SEQ ID NOs: 7-13. It should be appreciated that activity (e.g., specific activity) of an AcT can be measured by any means known to one of ordinary skill in the art. In some embodiments, activity (e.g., specific activity) of an AcT in a host cell may be measured as the concentration of phenyl acetate produced. In some embodiments, a polynucleotide encoding one or more of the AcTs associated with the disclosure is integrated into the genome of a host cell. In other embodiments, one or more of the AcTs associated with the disclosure is expressed on a plasmid in a host cell. Polynucleotides The term “heterologous” with respect to a polynucleotide, such as a polynucleotide comprising a gene, is used interchangeably with the term “exogenous” and the term “recombinant” and refers to: a polynucleotide that has been artificially supplied to a biological system such as a cell; a polynucleotide that has been modified within a biological system; or a polynucleotide whose expression or regulation has been manipulated within a biological system. A heterologous polynucleotide that is introduced into or expressed in a host cell may be a synthetic polynucleotide, a polynucleotide that comes from a different organism or species from the host cell, or a polynucleotide that results from modification or selective editing within the host cell of a polynucleotide that is endogenous to the host cell. A polynucleotide comprising a sequence that is endogenous to a host cell also may be considered heterologous when it is, for example: situated non-naturally in the host cell; expressed recombinantly in the host cell, either stably or transiently; present in a copy number that differs from the naturally occurring copy number within the host cell; or expressed in a non-natural way or at a non-natural level within the host cell, such as through manipulation of regulatory regions that control expression of the polynucleotide. In some embodiments, a heterologous polynucleotide is a polynucleotide that comprises a sequence endogenous to a host cell but whose expression is driven by a promoter that does not naturally regulate expression of the polynucleotide. In other embodiments, a heterologous polynucleotide is a polynucleotide that comprises a sequence endogenous to the host cell and whose expression is driven by a promoter that does naturally regulate expression of the polynucleotide, but the promoter driving its expression or another regulatory region regulating its expression has been modified. In some embodiments, the promoter is recombinantly activated or repressed. For example, gene-editing techniques may be used to regulate expression of a polynucleotide in a cell, including an endogenous polynucleotide, from a promoter, including an endogenous promoter. See, e.g., Chavez et al., Nat Methods.2016 Jul; 13(7): 563–567. A heterologous polynucleotide may comprise a wild-type sequence or a mutant sequence as compared with a reference polynucleotide sequence. A polynucleotide encoding a DC or an AcT associated with the disclosure may be incorporated into any appropriate vector through any method known in the art. For example, the vector may be an expression vector, including but not limited to a viral vector (e.g., a lentiviral, retroviral, adenoviral, or adeno-associated viral vector), any vector suitable for transient expression, any vector suitable for constitutive expression, or any vector suitable for inducible expression (e.g., a galactose-inducible or doxycycline-inducible vector). The vector may be a cloning vector, such as a plasmid, fosmid, phagemid, virus genome or artificial chromosome. As used in this application, the term "expression vector" or "expression construct" refers to a nucleic acid construct, generated recombinantly or synthetically, with a series of specified nucleic acid elements that permit transcription of a particular polynucleotide in a host cell, such as a yeast cell or bacterial cell. In some embodiments, a polynucleotide associated with the disclosure is inserted into an expression vector or expression construct such that it is operably joined to regulatory sequences and, in some embodiments, expressed as an RNA transcript. In some embodiments, the expression vector or expression construct contains one or more markers, such as a selectable marker, to identify cells transformed or transfected with the expression vector or expression construct. A polynucleotide encoding a polypeptide associated with the disclosure is “operably joined” or “operably linked” to a regulatory sequence when the polynucleotide and the regulatory sequence are covalently linked, and the expression or transcription of the polynucleotide is under the influence or control of the regulatory sequence. In some embodiments, a polynucleotide encoding any of the polypeptides described in this application is under the control of regulatory sequences (e.g., enhancer sequences). In some embodiments, a polynucleotide (e.g., a polynucleotide comprising a gene) is expressed under the control of a promoter. In some embodiments, the promoter is a native promoter, corresponding to the promoter of the gene in its endogenous context. In other embodiments, the promoter is not the native promoter of the gene, e.g., the promoter is different from the promoter of the gene in its endogenous context. In some embodiments, the promoter is a eukaryotic promoter. Non-limiting examples of eukaryotic promoters include TDH3, PGK1, PKC1, PDC1, TEF1, TEF2, RPL18B, SSA1, TDH2, PYK1,TPI1 GAL1, GAL10, GAL7, GAL3, GAL2, MET3, MET25, HXT3, HXT7, ACT1, ADH1, ADH2, CUP1-1, ENO2, and SOD1, as would be known to one of ordinary skill in the art (see, e.g., Addgene website: blog.addgene.org / plasmids-101-the-promoter-region). In some embodiments, the promoter is a prokaryotic promoter (e.g., bacteriophage or bacterial promoter). Non-limiting examples of bacteriophage promoters include Pls1con, T3, T7, SP6, and PL. Non-limiting examples of bacterial promoters include Pbad, PmgrB, Ptrc2, Plac / ara, Ptac, and Pm. In some embodiments, the promoter is an inducible promoter. As used in this application, an “inducible promoter” is a promoter controlled by the presence or absence of a molecule. Non-limiting examples of inducible promoters include chemically regulated promoters and physically regulated promoters. For chemically regulated promoters, the transcriptional activity can be regulated by one or more compounds, such as alcohol, an antibiotic such as tetracycline, a carbon source such as galactose, a steroid, a metal, or other compounds. For physically regulated promoters, transcriptional activity can be regulated by a phenomenon such as light or temperature. Non-limiting examples of tetracycline-regulated promoters include anhydrotetracycline (aTc)-responsive promoters and other tetracycline- responsive promoter systems (e.g., a tetracycline repressor protein (tetR), a tetracycline operator sequence (tetO) and a tetracycline transactivator fusion protein (tTA)). Non-limiting examples of steroid-regulated promoters include promoters based on the rat glucocorticoid receptor, human estrogen receptor, moth ecdysone receptors, and promoters from the steroid / retinoid / thyroid receptor superfamily. Non-limiting examples of metal-regulated promoters include promoters derived from metallothionein (proteins that bind and sequester metal ions) genes. Non-limiting examples of pathogenesis-regulated promoters include promoters induced by salicylic acid, ethylene or benzothiadiazole (BTH). Non-limiting examples of temperature / heat-inducible promoters include heat shock promoters. Non-limiting examples of light-regulated promoters include light responsive promoters from plant cells. In certain embodiments, the inducible promoter is a galactose-inducible promoter. In some embodiments, the inducible promoter is induced by one or more physiological conditions (e.g., pH, temperature, radiation, osmotic pressure, saline gradients, cell surface binding, or concentration of one or more extrinsic or intrinsic inducing agents). Non-limiting examples of an extrinsic inducer or inducing agent include amino acids and amino acid analogs, saccharides and polysaccharides, nucleic acids, protein transcriptional activators and repressors, cytokines, toxins, petroleum-based compounds, metal containing compounds, salts, ions, enzyme substrate analogs, hormones or any combination thereof. In some embodiments, the promoter is a constitutive promoter. As used in this application, a “constitutive promoter” refers to an unregulated promoter that allows continuous transcription of a gene. Non-limiting examples of a constitutive promoter include TDH3, PGK1, PKC1, PDC1, TEF1, TEF2, RPL18B, SSA1, TDH2, PYK1, TPI1, HXT3, HXT7, ACT1, ADH1, ADH2, ENO2, and SOD1. Other inducible promoters or constitutive promoters known to one of ordinary skill in the art are also contemplated. In some embodiments, introduction of a polynucleotide, such as a polynucleotide encoding an AcT and / or a DC associated with the disclosure, into a host cell results in genomic integration of the polynucleotide. In some embodiments, a host cell (e.g., a yeast cell or a bacterial cell) comprises at least 1 copy, at least 2 copies, at least 3 copies, at least 4 copies, at least 5 copies, at least 6 copies, at least 7 copies, at least 8 copies, at least 9 copies, at least 10 copies, at least 11 copies, at least 12 copies, at least 13 copies, at least 14 copies, at least 15 copies, at least 16 copies, at least 17 copies, at least 18 copies, at least 19 copies, at least 20 copies, at least 21 copies, at least 22 copies, at least 23 copies, at least 24 copies, at least 25 copies, at least 26 copies, at least 27 copies, at least 28 copies, at least 29 copies, at least 30 copies, at least 31 copies, at least 32 copies, at least 33 copies, at least 34 copies, at least 35 copies, at least 36 copies, at least 37 copies, at least 38 copies, at least 39 copies, at least 40 copies, at least 41 copies, at least 42 copies, at least 43 copies, at least 44 copies, at least 45 copies, at least 46 copies, at least 47 copies, at least 48 copies, at least 49 copies, at least 50 copies, at least 60 copies, at least 70 copies, at least 80 copies, at least 90 copies, at least 100 copies, or more, including any values in between, of a polynucleotide sequence, such as a polynucleotide sequence encoding any of the polypeptides described in this application, in its genome. Said copies may be inserted into the same locus or into different loci of a host cell of the disclosure. In some embodiments, the sequence of a polynucleotide (e.g., a polynucleotide comprising a gene) is codon optimized. Codon optimization may increase expression of a gene by at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100%, including all values in between) relative to a reference sequence that is not codon-optimized. In some embodiments, a polynucleotide encoding an AcT comprises a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to any one of SEQ ID NOs: 9-13. In some embodiments, a polynucleotide encoding an AcT comprises the sequence of any one of SEQ ID NOs: 9-13. In some embodiments, a polynucleotide encoding a DC comprises a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical, including all values in between, to any one of SEQ ID NOs: 20-22. In some embodiments, a polynucleotide encoding a DC comprises the sequence of any one of SEQ ID NOs: 20-22. 3. Percent Identity Aspects of the disclosure relate to variant AcTs or variant DCs. As used in this disclosure, a "variant" polynucleotide refers to a polynucleotide that differs from a reference polynucleotide by one or more nucleotides in its sequence. As used in this disclosure, a "variant" polypeptide refers to a polypeptide that differs from a reference polypeptide by one or more amino acids in its sequence. A variant may share at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity with a reference sequence, including all values in between. Unless otherwise noted, the term “sequence identity” refers to the relatedness of the sequences of two polypeptides or polynucleotides when the sequences are aligned, and the term “percent identity” refers to the percentage of residues (amino acids or nucleotides) that are identical when two polypeptide or polynucleotide sequences are aligned. In some embodiments, sequence identity and / or percent identity is determined across the entire length of a sequence, while in other embodiments, sequence identity and / or percent identity is determined over a region of a sequence. Percent identity of polypeptide or polynucleotide sequences can be calculated by any of the methods known to one of ordinary skill in the art. For example, percent identity can be determined using the algorithm of Karlin and Altschul Proc. Natl. Acad. Sci. USA 87:2264-68, 1990, modified as in Karlin and Altschul Proc. Natl. Acad. Sci. USA 90:5873-77, 1993. Such an algorithm is incorporated into the NBLAST®and XBLAST®programs (version 2.0) of Altschul et al., J. Mol. Biol.215:403-10, 1990. BLAST®protein searches can be performed, for example, with the XBLAST program, score=50, wordlength=3. Where gaps exist between two sequences, Gapped BLAST®can be utilized, for example, as described in Altschul et al., Nucleic Acids Res. 25(17):3389-3402, 1997. When utilizing BLAST®and Gapped BLAST®programs, the default parameters of the respective programs (e.g., XBLAST®and NBLAST®) can be used, or the parameters can be adjusted appropriately as would be understood by one of ordinary skill in the art. A second example of a local alignment technique is based on the Smith-Waterman algorithm (Smith, T.F. & Waterman, M.S. (1981) J. Mol. Biol.147:195-197). An example of a global alignment technique is the Needleman–Wunsch algorithm (Needleman, S.B. & Wunsch, C.D. (1970) J. Mol. Biol.48:443-453), which is based on dynamic programming. A further example of a global alignment technique is the Fast Optimal Global Sequence Alignment Algorithm (FOGSAA). In some embodiments, the identity of two polypeptide sequences is determined by aligning the amino acid sequences of the polypeptides, calculating the number of identical amino acids, and dividing by the length of one of the polypeptide sequences. In some embodiments, the identity of two polynucleotide sequences is determined by aligning the nucleic acid sequences of the polynucleotides, calculating the number of identical nucleic acids and dividing by the length of one of the polynucleotide sequences. For multiple sequence alignments, computer programs including Clustal Omega (Sievers et al., Mol Syst Biol.2011 Oct 11;7:539) may be used. In some embodiments, sequence identity is determined using the algorithm of Karlin and Altschul Proc. Natl. Acad. Sci. USA 87:2264-68, 1990, modified as in Karlin and Altschul Proc. Natl. Acad. Sci. USA 90:5873-77, 1993 (e.g., BLAST®, NBLAST®, XBLAST® or Gapped BLAST® programs, using default parameters of the respective programs). In some embodiments, the sequence identity of two amino acid or polynucleotide sequences is determined using the Smith-Waterman algorithm (Smith, T.F. & Waterman, M.S. (1981) J. Mol. Biol.147:195-197) or the Needleman–Wunsch algorithm (Needleman, S.B. & Wunsch, C.D. (1970) J. Mol. Biol.48:443-453). In some embodiments, the sequence identity of two amino acid or polynucleotide sequences is determined using a Fast Optimal Global Sequence Alignment Algorithm (FOGSAA). In some embodiments, the sequence identity of two amino acid or polynucleotide sequences is determined using Clustal Omega (Sievers et al., Mol Syst Biol.2011 Oct 11;7:539). As used in this application, a residue (such as a nucleic acid residue or an amino acid residue) in sequence “X” is referred to as corresponding to a position or residue (such as a nucleic acid residue or an amino acid residue) “Z” in a different sequence “Y” when the residue in sequence “X” is at the counterpart position of “Z” in sequence “Y” when sequences X and Y are aligned using sequence alignment tools known in the art. Variant sequences may be homologous sequences. As used in this application, homologous sequences are sequences (e.g., nucleic acid or amino acid sequences) that share a certain percent identity (e.g., at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% percent identity, including all values in between) and may be paralogous sequences, orthologous sequences, or sequences arising from convergent evolution. Paralogous sequences arise from duplication of a gene within a genome of a species, while orthologous sequences diverge after a speciation event. Two different species may have evolved independently but may each comprise a sequence that shares a certain percent identity with a sequence from the other species as a result of convergent evolution. In some embodiments, a polypeptide variant (e.g., an AcT variant or a DC variant) comprises the same or substantially similar secondary structure (e.g., alpha helix, beta sheet) as that of a reference polypeptide (e.g., a reference AcT or a reference DC). In some embodiments, a polypeptide variant (e.g., an AcT variant or a DC variant) comprises the same or substantially similar tertiary structure as that of a reference polypeptide (e.g., a reference AcT or a reference DC). As a non-limiting example, a variant polypeptide may have low primary sequence identity (e.g., less than 80%, less than 75%, or less than 70% sequence identity) compared to a reference polypeptide, but comprises one or more secondary structures (e.g., including but not limited to loops, alpha helices, or beta sheets) or the same tertiary structure as that of a reference polypeptide. For example, a loop may be located between a beta sheet and an alpha helix, between two alpha helices, or between two beta sheets. Homology modeling may be used to compare two or more tertiary structures. In some embodiments, an algorithm that determines the percent identity between a sequence of interest and a reference sequence described in this application accounts for the presence of circular permutation between the sequences. The presence of circular permutation may be detected using any method known in the art, including, for example, RASPODOM (Weiner et al., Bioinformatics 2005 Apr 1;21(7):932-7). In some embodiments, the presence of circulation permutation is corrected for (e.g., the domains in at least one sequence are rearranged) prior to calculation of the percent identity between a sequence of interest and a sequence described in this application. Functional variants of AcTs and / or DCs disclosed in this application are also encompassed by the present disclosure. For example, functional variants may bind one or more of the same substrates (e.g., 4-HB or phenol) or produce one or more of the same products (e.g., phenol or phenyl acetate). Functional variants may be identified using any method known in the art. For example, the algorithm of Karlin and Altschul Proc. Natl. Acad. Sci. USA 87:2264-68, 1990 described above may be used to identify homologous proteins. 4. Host Cells Any of the polynucleotides or polypeptides of the disclosure may be expressed in a host cell. As used in this application, the term “host cell” refers to a cell that can be used to express a polynucleotide, such as a polynucleotide that encodes a polypeptide used in production of phenyl acetate. Any suitable host cell may be used to express any of the recombinant polypeptides, including an AcT or a DC, and other polypeptides disclosed in this application, including eukaryotic cells or prokaryotic cells. Aspects of the disclosure provide a suitable host cell expressing at least one heterologous AcT and at least one heterologous DC. Suitable host cells include, but are not limited to, fungal cells (e.g., yeast cells), bacterial cells (e.g., E. coli cells), algal cells, plant cells, insect cells, and animal cells, including mammalian cells. Suitable yeast host cells include, but are not limited to: Candida, Hansenula, Saccharomyces, Schizosaccharomyces, Pichia, Kluyveromyces, and Yarrowia. In some embodiments, the yeast cell is Hansenula polymorpha, Saccharomyces cerevisiae, Saccharomyces carlsbergensis, Saccharomyces diastaticus, Saccharomyces norbensis, Saccharomyces kluyveri, Schizosaccharomyces pombe, Pichia pastoris, Pichia finlandica, Pichia trehalophila, Pichia kodamae, Pichia membranaefaciens, Pichia opuntiae, Pichia thermotolerans, Pichia salictaria, Pichia quercuum, Pichia pijperi, Pichia stipitis, Pichia methanolica, Pichia angusta, Kluyveromyces lactis, Candida albicans, or Yarrowia lipolytica. In some embodiments, the yeast strain is an industrial polyploid yeast strain. Other non- limiting examples of fungal cells include cells obtained from Aspergillus spp., Penicillium spp., Fusarium spp., Rhizopus spp., Acremonium spp., Neurospora spp., Sordaria spp., Magnaporthe spp., Allomyces spp., Ustilago spp., Botrytis spp., and Trichoderma spp. In other embodiments, the host cell is a prokaryotic cell. Suitable prokaryotic cells include gram positive, gram negative, and gram-variable bacterial cells. The host cell may be a species of, but not limited to: Agrobacterium, Alicyclobacillus, Anabaena, Anacystis, Acinetobacter, Acidothermus, Arthrobacter, Azotobacter, Bacillus, Bifidobacterium, Brevibacterium, Butyrivibrio, Buchnera, Campestris, Campylobacter, Clostridium, Corynebacterium, Chromatium, Coprococcus, Escherichia, Enterococcus, Enterobacter, Erwinia, Fusobacterium, Faecalibacterium, Francisella, Flavobacterium, Geobacillus, Haemophilus, Helicobacter, Klebsiella, Lactobacillus, Lactococcus, Ilyobacter, Micrococcus, Microbacterium, Mesorhizobium, Methylobacterium, Methylobacterium, Mycobacterium, Neisseria, Pantoea, Pseudomonas, Prochlorococcus, Rhodobacter, Rhodopseudomonas, Rhodopseudomonas, Roseburia, Rhodospirillum, Rhodococcus, Scenedesmus, Streptomyces, Streptococcus, Synecoccus, Saccharomonospora, Saccharopolyspora, Staphylococcus, Serratia, Salmonella, Shigella, Thermoanaerobacterium, Tropheryma, Tularensis, Temecula, Thermosynechococcus, Thermococcus, Ureaplasma, Xanthomonas, Xylella, Yersinia, and Zymomonas. In some embodiments, the bacterial host strain is an industrial strain. Numerous bacterial industrial strains are known and suitable for the methods and compositions described in this application. In some embodiments, the bacterial host cell is of the Agrobacterium species (e.g., A. radiobacter, A. rhizogenes, A. rubi), the Arthrobacter species (e.g., A. aurescens, A. citreus, A. globformis, A. hydrocarboglutamicus, A. mysorens, A. nicotianae, A. paraffineus, A. protophonniae, A. roseoparaffinus, A. sulfureus, A. ureafaciens), the Bacillus species (e.g., B. thuringiensis, B. anthracis, B. megaterium, B. subtilis, B. lentus, B. circulars, B. pumilus, B. lautus, B. coagulans, B. brevis, B. firmus, B. alkaophius, B. licheniformis, B. clausii, B. stearothermophilus, B. halodurans, B. amyloliquefaciens). In particular embodiments, the host cell will be an industrial Bacillus strain including but not limited to B. subtilis, B. pumilus, B. licheniformis, B. megaterium, B. clausii, B. stearothermophilus and B. amyloliquefaciens. In some embodiments, the host cell will be an industrial Clostridium species (e.g., C. acetobutylicum, C. tetani E88, C. lituseburense, C. saccharobutylicum, C. perfringens, C. beijerinckii). In some embodiments, the host cell will be an industrial Corynebacterium species (e.g., C. glutamicum, C. acetoacidophilum). In some embodiments, the host cell will be an industrial Escherichia species (e.g., E. coli). In some embodiments, the host cell will be an industrial Erwinia species (e.g., E. uredovora, E. carotovora, E. ananas, E. herbicola, E. punctata, E. terreus). In some embodiments, the host cell will be an industrial Pantoea species (e.g., P. citrea, P. agglomerans). In some embodiments, the host cell will be an industrial Pseudomonas species, (e.g., P. putida, P. aeruginosa, P. mevalonii). In some embodiments, the host cell will be an industrial Streptococcus species (e.g., S. equisimiles, S. pyogenes, S. uberis). In some embodiments, the host cell will be an industrial Streptomyces species (e.g., S. ambofaciens, S. achromogenes, S. avermitilis, S. coelicolor, S. aureofaciens, S. aureus, S. fungicidicus, S. griseus, S. lividans). In some embodiments, the host cell will be an industrial Zymomonas species (e.g., Z. mobilis, Z. lipolytica). In various embodiments, cell types or strains that may be used in the practice of the disclosure including both prokaryotic and eukaryotic cell or strains, and are readily accessible to the public from a number of culture collections such as American Type Culture Collection (ATCC), Deutsche Sammlung von Mikroorganismen and Zellkulturen GmbH (DSM), Centraalbureau Voor Schimmelcultures (CBS), and Agricultural Research Service Patent Culture Collection, Northern Regional Research Center (NRRL). The term “cell,” as used in this application, may refer to a single cell or a population of cells, such as a population of cells belonging to the same cell line or strain. Use of the singular term “cell” should not be construed to refer explicitly to a single cell rather than a population of cells. The host cell may comprise genetic modifications relative to a wild-type counterpart. Any suitable host cell may be used to express any of the polypeptides (e.g., a DC or an AcT) disclosed in this application to produce phenyl acetate, including eukaryotic cells or prokaryotic cells. In some embodiments, a host cell that expresses a heterologous polynucleotide encoding a DC or an AcT disclosed herein may increase phenyl acetate production by approximately 1.1- fold, 1.2-fold, 1.3-fold, 1.4-fold, 1.5-fold, 2-fold, 2.5-fold, 3-fold, 3.5-fold, 4-fold, 4.5-fold, 5- fold, 5.5-fold, or 6-fold more (e.g., 2-fold to 6-fold more) or by or at least about 0.2, 0.4, 0.6, 0.8, 1, 2, 3, 4, 5, 6 or 7 mg / L relative to a control. In some embodiments, the control is a host cell that does not express a heterologous polynucleotide encoding a DC or an AcT. In some embodiments, a host cell comprises a heterologous polynucleotide encoding a DC that comprises an amino acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to SEQ ID NO: 14. In some embodiments, a host cell comprises a heterologous polynucleotide encoding a DC that comprises the amino acid sequence of SEQ ID NO: 14. In some embodiments, a host cell comprises a heterologous polynucleotide encoding a DC that comprises an amino acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to SEQ ID NO: 15. In some embodiments, a host cell comprises a heterologous polynucleotide encoding a DC that comprises the amino acid sequence of SEQ ID NO: 15. In some embodiments, a host cell comprises a heterologous polynucleotide encoding a DC that comprises an amino acid sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identical to SEQ ID NO: 16. In some embodiments, a host cell comprises a heterologous polynucleotide encoding a DC that comprises the amino acid sequence of SEQ ID NO: 16. In some embodiments, a host cell comprises a heterologous polynucleotide that comprises a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to any one of SEQ ID NOs: 17-22. In some embodiments, a host cell comprises a heterologous polynucleotide that comprises the sequence of any one of SEQ ID NOs: 17-22. In some embodiments, a host cell comprising a heterologous polynucleotide encoding a DC is not a bacterial cell. In some embodiments, a host cell comprising a heterologous polynucleotide encoding a DC is a yeast cell (e.g., a Saccharomyces cell). In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the sequence of SEQ ID NO: 1. In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises the amino acid sequence of SEQ ID NO: 1. In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the sequence of SEQ ID NO: 2. In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises the amino acid sequence of SEQ ID NO: 2. In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the sequence of SEQ ID NO: 3. In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises the amino acid sequence of SEQ ID NO: 3. In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the sequence of SEQ ID NO: 4. In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises the amino acid sequence of SEQ ID NO: 4. In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the sequence of SEQ ID NO: 5 In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises the amino acid sequence of SEQ ID NO: 5. In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the sequence of SEQ ID NO: 6. In some embodiments, a host cell comprises a heterologous polynucleotide encoding an AcT that comprises the amino acid sequence of SEQ ID NO: 6. In some embodiments, a host cell comprises a heterologous polynucleotide that comprises a sequence that is at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to any one of SEQ ID NOs: 7-13. In some embodiments, a host cell comprises a heterologous polynucleotide that comprises the sequence of any one of SEQ ID NOs: 7-13. In some embodiments, the suitable host cell may further include one or more additional copies of one or more polynucleotides encoding one or more glycolytic enzymes, enzymes of the PPP pathway, enzymes of the shikimate pathway, or any combination thereof, for the biosynthesis of phenol or phenylacetate from glucose. 5. Combinations Aspects of the disclosure provide host cells that comprise one or more heterologous polynucleotides collectively encoding (i) a 4-hydroxybenzoate decarboxylase (4-HB DC) and (ii) an acetyl transferase (AcT), wherein the host cell is capable of converting hydroxybenzoate to phenol and of converting phenol to phenyl acetate. In some embodiments, the 4-HB DC and AcT are encoded by a single polynucleotide. In some embodiments, the 4-HB DC and AcT are each encoded on a separate polynucleotide. In some embodiments, a host cell comprises one or more heterologous polynucleotides collectively encoding a 4-HB DC and two or more AcTs. In some embodiments, the one or more heterologous polynucleotides collectively encode a 4-HB DC and two AcTs, three AcTs, four AcTs, five AcTs, six AcTs, seven AcTs, eight AcTs, nine AcTs, or ten AcTs. In some embodiments, a host cell comprises one or more heterologous polynucleotides collectively encoding a 4-HB DC and two or more of: an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 1; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 2; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 3; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 4; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 5; and an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 6. In some embodiments, a host cell comprises one or more heterologous polynucleotides collectively encoding one or more 4-HB DC and at least one AcT. In some embodiments, a host cell comprises one or more heterologous polynucleotides collectively encoding two or more 4- HB DCs and at least one AcT. In some embodiments, the one or more heterologous polynucleotides collectively encode at least one 4-HB DC and two AcTs, three AcTs, four AcTs, five AcTs, six AcTs, seven AcTs, eight AcTs, nine AcTs, or ten AcTs. In some embodiments, the one or more heterologous polynucleotides collectively encode at least two 4-HB DCs and two AcTs, three AcTs, four AcTs, five AcTs, six AcTs, seven AcTs, eight AcTs, nine AcTs, or ten AcTs. In some embodiments, a host cell comprises one or more heterologous polynucleotides collectively encoding at least one AcT and two or more of: a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 14; a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO:15; and a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 16. In some embodiments, a host cell comprises one or more heterologous polynucleotides collectively encoding (i) two or more of: a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 14; a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO:15; and a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 16, and (ii) two or more of: an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 1; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 2; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 3; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 4; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 5; and an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 6. Aspects of the disclosure provide host cells comprising one or more heterologous polynucleotides collectively encoding one or more AcTs. In some embodiments, a host cell comprises one or more heterologous polynucleotides collectively encoding two or more AcTs. In some embodiments, the one or more heterologous polynucleotides collectively encode two AcTs, three AcTs, four AcTs, five AcTs, six AcTs, seven AcTs, eight AcTs, nine AcTs, or ten AcTs. In some embodiments, a host cell comprises one or more heterologous polynucleotides collectively encoding two or more of, three or more of, four or more of, five or more of, or each of: an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 1; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 2; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 3; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 4; an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 5; and an AcT having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 6. Aspects of the disclosure provide host cells comprising one or more heterologous polynucleotides collectively encoding one or more 4-HB DCs, wherein the host cell is not a bacterial host cell. In some embodiments, a host cell comprises one or more heterologous polynucleotides collectively encoding two or more 4-HB DCs. In some embodiments, the one or more heterologous polynucleotides collectively encode two 4-HB DCs, three 4-HB DCs, four 4- HB DCs, five 4-HB DCs, six 4-HB DCs, seven 4-HB DCs, eight 4-HB DCs, nine 4-HB DCs, or ten 4-HB DCs. In some embodiments, a host cell comprises one or more heterologous polynucleotides collectively encoding (i) two or more of or each of: a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 14; a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO:15; and a 4-HB DC having a sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to SEQ ID NO: 16. Aspects of the disclosure provide host cells comprising one or more heterologous polynucleotides collectively encoding one or more additional copies of one or more polynucleotides encoding one or more glycolytic enzymes, enzymes of the PPP pathway, enzymes of the shikimate pathway, or any combination thereof, for the biosynthesis of phenol or phenylacetate from glucose. 6. Additional Genetic Modifications Aspects of the disclosure provide host cells that comprise genetic modifications relative to a wild-type counterpart. As a non-limiting example, a host cell (e.g., S. cerevisiae) may be modified to reduce or inactivate one or more endogenous genes encoding an esterase. In some embodiments the gene encoding an esterase is selected from: SAY1 and / or IAH1. In some embodiments, a host cell comprises one or more genetic modifications that result in decreased expression, relative to a control host cell lacking the one or more genetic modifications, of at least one endogenous gene. In some embodiments, a host cell comprises one or more genetic modifications that result in decreased expression, relative to a control host cell lacking the one or more genetic modifications, of at least one endogenous gene encoding an esterase. In some embodiments, a host cell comprises one or more genetic modifications that result in decreased expression, relative to a control host cell lacking the one or more genetic modifications, of at least one endogenous gene encoding an esterase, wherein the gene encoding an esterase is selected from SAY1 and IAH1. In some embodiments, a host cell comprising one or more genetic modifications that result in decreased expression of an endogenous gene encoding an esterase produces more phenyl acetate than a control host cell without the one or more genetic modifications. In some embodiments, a host cell comprising one or more genetic modifications that result in decreased expression of an endogenous gene encoding an esterase produces at least about 5X, 10X, 50X, or 100X more phenyl acetate, or at least about 0.2, 0.4, 0.6, 0.8, 1, 2, 3, 4, 5, 6 or 7 mg / L more phenyl acetate than the control host cell. In some embodiments, a host cell is modified to reduce or inactivate at least 1, at least 2, at least 3, at least 4, at least 5, at least 6, at least 7, at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14, at least 15, at least 16, at least 17, at least 18, at least 19, or at least 20 genes. In some embodiments, a host cell is modified to reduce or inactivate 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 genes. Reduction of gene expression and / or gene inactivation may be achieved through any suitable method, including but not limited to deletion of the gene, introduction of a point mutation into the gene, truncation of the gene, introduction of an insertion into the gene, introduction of a tag or fusion into the gene, or selective editing of the gene. For example,polymerase chain reaction (PCR)-based methods may be used (see ̧e.g., Gardner et al., MethodsMol Biol.2014;1205:45-78) or well-known gene-editing techniques may be used. As a non- limiting example, genes may be deleted through gene replacement (e.g., with a marker, including a selection marker). A gene may also be truncated through the use of a transposon system (see, e.g., Poussu et al., Nucleic Acids Res.2005; 33(12): e104). In some embodiments, the one or more genetic modifications comprise a knockout of an endogenous gene. In some embodiments, the one or more genetic modifications comprise a knockout of an endogenous gene encoding an esterase. In some embodiments, the one or more genetic modifications comprise a knockout of SAY1 and / or a knockout of IAH1. In some embodiments, a host cell comprising one or more genetic modifications comprising a knockout of an endogenous gene encoding an esterase produces more phenyl acetate than a control host cell without the one or more genetic modifications. In some embodiments, a host cell comprising one or more genetic modifications comprising a knockout of an endogenous gene encoding an esterase produces 5X, 10X, 50X, or 100X more phenyl acetate, or at least 0.2, 0.4, 0.6, 0.8, 1, 2, 3, 4, 5, 6 or 7 mg / L more phenyl acetate than a control host cell. A vector or polynucleotide encoding any of the polypeptides described in this application may be introduced into a suitable host cell using any method known in the art. Non-limiting examples of yeast transformation protocols are described in Gietz et al., Yeast transformation can be conducted by the LiAc / SS Carrier DNA / PEG method. Methods Mol Biol.2006; 313:107- 20, which is incorporated by reference in its entirety. Host cells may be cultured under any suitable conditions as would be understood by one of ordinary skill in the art. For example, any media, temperature, and incubation conditions known in the art may be used. For host cells carrying an inducible vector, cells may be cultured with an appropriate inducible agent to promote expression. 7. Methods Aspects of the disclosure provide, at least in part, methods for producing a bioproduct using host cells associated with the disclosure. In some embodiments, cells associated with the disclosure are used to make phenyl acetate. In some embodiments, a method for producing phenyl acetate comprises culturing a host cell of the present disclosure. Any of the cells disclosed in this application can be cultured in media of any type (rich or minimal) and any composition prior to, during, and / or after contact and / or integration of a nucleic acid. The conditions of the culture or culturing process can be optimized through routine experimentation as would be understood by one of ordinary skill in the art. In some embodiments, the selected media is supplemented with various components. In some embodiments, the concentration and amount of a supplemental component is optimized. In some embodiments, other aspects of the media and growth conditions (e.g., pH, temperature, etc.) are optimized through routine experimentation. In some embodiments, the frequency that the media is supplemented with one or more supplemental components, and the amount of time that the cell is cultured, is optimized. Culturing of the cells described in this application can be performed in culture vessels known and used in the art. In some embodiments, an aerated reaction vessel (e.g., a stirred tank reactor) is used to culture the cells. In some embodiments, a bioreactor or fermenter is used to culture the cells. Thus, in some embodiments, the cells are used in fermentation. As used in this application, the terms “bioreactor” and “fermenter” are interchangeably used and refer to an enclosure, or partial enclosure, in which a biological, biochemical and / or chemical reaction takes place, involving a living organism, part of a living organism, or purified proteins. Any type of bioreactor or fermenter known in the art may be compatible with aspects of the disclosure, including large or industrial scale bioreactors such as those with volumes in the range of liters or hundreds or thousands of liters or more. In some embodiments, the method involves batch fermentation (e.g., shake flask fermentation). General considerations for batch fermentation (e.g., shake flask fermentation) include the level of oxygen and glucose. For example, batch fermentation (e.g., shake flask fermentation) may be oxygen and glucose limited, so in some embodiments, the capability of a strain to perform in a well-designed fed-batch fermentation is underestimated. Also, the final product (e.g., phenyl acetate or phenol) may display some differences from the substrate (e.g., 4- HB) in terms of solubility, toxicity, cellular accumulation and secretion and in some embodiments can have different fermentation kinetics. In some embodiments, host cells are cultured in media that is buffered to pH 5. In some embodiments, host cells are cultured in media that is buffered to pH 5, and after host cell growth, the pH drops to about 4.5. In some embodiments, host cells are cultured at a pH between about 4.5 to about 5.5. In some embodiments, host cells of the present disclosure are cultured at a pH of about 6 or below. In some embodiments, host cells are cultured at a pH between 6.5 and 5.5, 6.25 and 5.25, 6 and 5, 6.5 and 5.9, 6.4 and 5.7, or 6.1 and 5.9. In some embodiments, host cells are cultured at a pH of about 7. In some embodiments, the method further comprises isolating phenyl acetate from the cell culture. In some embodiments, phenyl acetate is isolated due to its lower density relative to the cell culture. In some embodiments, phenyl acetate produced by host cells associated with the disclosure is further converted to phenol. 8. Purification of phenyl acetate from host cells and subsequent conversion of phenyl acetate to phenol Following the production of phenyl acetate in host cells, the phenyl acetate can be purified using any of various methods known in the art, the phenyl acetate can be readily converted into phenol. Simple one-step reactions to produce phenol from phenyl acetate include the Photo-Fries rearrangement; see: Kalmus et al.1974 J. Am. Chem. Soc.2: 449; and Toldo et al.2017 Phys. Chem. Chem. Phys.29: 19103. Simple acid hydrolysis of the ester bond can also be performed. Hydrolysis of the ester bond could also occur in the same fermentation vessel by simple acid addition and lowering of the pH. The phraseology and terminology used in this application is for the purpose of description and should not be regarded as limiting. The use of terms such as “including,” “comprising,” “having,” “containing,” “involving,” and / or variations thereof in this application, is meant to encompass the items listed thereafter and equivalents thereof as well as additional items. The present invention is further illustrated by the following Examples, which in no way should be construed as further limiting. The entire contents of all of the references (including literature references, issued patents, published patent applications, and co-pending patent applications) cited throughout this application are hereby expressly incorporated by reference. EXAMPLES Example 1. Methods for Detecting Phenol, Phenyl acetate (PA), and 4-hyroxybenzoate (4-HB) This example highlights three assays that were developed to detect active decarboxylase and acetyltransferases. The constructs containing various decarboxylases (about 20 distinct DCs) were transformed into S. cerevisiae, where the empty strain or wildtype (WT) was used as the negative control. Single transformants were picked and cultured in 300 μL of minimal media with 4% dextrose to prepare preculture samples. The pre-cultures were shaken and grown at 30 °C, 1000 rpm for 48 hours. After the incubation period, 10 μL of preculture was inoculated into 300 μL of production minimal media with 2% raffinose and 2% galactose. The production cultures were shaken and grown at 30 °C, 1000 rpm for 48 hours. After 48 hours, 10 μL of proculture samples were diluted into 190 μL of dilution buffer. Samples were centrifuged at 4000 X g for 10 min and subsequently, 50 μL of diluted samples were transferred to EchoPP plates to be run on Echo® MS+ system with SCIEX Triple Quad 6500+ system for phenol and 4-HB detection. Samples were acoustically ejected at 10 nL / replicate and run in a mobile phase of 45% acetonitrile, 45% methanol, 10 % LC-MS water and 0.1 % ammonium hydroxide. The library containing 500 various acetyltransferases were transformed into S. cerevisiae, where the empty strain or WT was used as the negative control. Single transformants were picked and cultured in 300 μL of minimal media with 4% dextrose to prepare preculture samples. The pre-cultures were shaken and grown at 30 °C, 1000 rpm for 48 hours. After the incubation period, 10 μL of preculture was inoculated into 300 μL of production minimal media with 2% raffinose and 2% galactose. The production cultures were shaken and grown at 30 °C, 1000 rpm for 24 hours. After 24 hours, 100 μL of proculture media with 2 g / L of phenol was added to glass-coated plates, then 300 μL of proculture samples were then transferred to 96w glass-coated plates. The proculture samples were incubated at 30 °C, 1000 rpm for 24 hours. Samples were transferred to a 2 mL deep well 96w plate where they were lysed with bead- beating and an equivolume of ethyl acetate. After bead beating, the samples were centrifuged at 4000 X g for 10 mins and the ethyl acetate layer was added to glass vials to be run on a Thermo Gas Chromatograph with Flame Ionization Detector using a Thermo TG-5MS (15m x 0.250mm x 0.250µm) column with helium as the carrier gas for phenol, phenyl acetate and 4- hydroxybenzoate detection. In the detection of engineered S. cerevisiae strains, where strains contained 4- hydroxybenzoate decarboxylase and acetyltransferase enzymes, the empty strain or WT was used as the negative control. Single transformants were picked and cultured in 300 μL of minimal media with 4% dextrose to prepare preculture samples. The pre-cultures were shaken and grown at 30 °C, 1000 rpm for 48 hours. After the incubation period, 10 μL of preculture was inoculated into 300 μL of production minimal media with 2% raffinose and 2% galactose. The production cultures were shaken and grown at 30 °C, 1000 rpm for 24 hours. After 24 hours, 100 μL of proculture media with 2 g / L of phenol was added to glass-coated plates, then 300 μL of proculture samples were then transferred to 96w glass-coated plates incubated at 30 °C, 1000 rpm for 24 hours. The proculture samples were prepared to be run on the EchoMS+ and GC-MS. First, 10 μL of proculture samples were diluted into 190 μL of dilution buffer. Diluted samples were centrifuged at 4000 X g for 10 min and subsequently, 50 μL of diluted samples were transferred to EchoPP plates to be run on Echo® MS+ system with SCIEX Triple Quad 6500+ system for phenol and 4-HB detection. Samples were acoustically ejected at 10 nL / replicate and run in a mobile phase of 45% acetonitrile, 45% methanol, 10 % LC-MS water and 0.1 % ammonium hydroxide. Remaining proculture samples were transferred to a 2 mL deep well 96w plate where they were lysed with bead-beating and an equivolume of ethyl acetate. After bead beating, the samples were centrifuged at 4000 G for 10 mins and the ethyl acetate layer was added to glass vials to be run on an Agilent GC-MS 6 (MASSX - 28) using a Thermo TG-5MS (15m x 0.250mm x 0.250µm) column with helium as the carrier gas for phenol, phenyl acetate and 4-hydroxybenzoate detection. Example 2. Identification of a 4-HB Decarboxylase Decarboxylase (DC) capable of converting 4-hydroxybenzoate to phenol in a cell was identified as follows. The engineered S. cerevisiae (containing four copies of the Klebsiella pneumoniae 4-HB Decarboxylase) cells were cultured in minimal media under the conditions discussed in Example 1. Around 20 S. cerevisiae strains containing distinct DCs were generated and tested for the decarboxylation activity on 4-HB. The DCs in each strain were expressed via galactose induction. When 4-hydroxybenzoate was fed into the assay containing the expressed DCs at the given concentration (500 mg / L), a very high conversion (>75%) to phenol was observed with the strain containing the K. pneumoniae 4HB-DC (FIG.2). The genotypes of the strains shown in FIG.2 are as follows: t1894825: Acyltransferase | Mycobacterium smegmatis str. MC2155 t1894827: Benzoyltransferase | Petunia x hybrida t1894829: 4-hydroxybenzoate decarboxylase | Klebsiella pneumoniae t1894834: 4-hydroxybenzoate decarboxylase | Klebsiella pneumoniae and Acyltransferase | Mycobacterium smegmatis str. MC2155 Strains comprising the Klebsiella pneumoniae 4-HB DC (e.g., t1894829 and t1894834) produced high levels of phenol. The sequences of the DCs with the highest activity are shown in Table 2 below.

[0002] ).A C C AAAAAC A CC CGAACA CT ATA AACA A TTGT AG TTA O A G A A TACGT C GA TAAA AG N AAA CAT GT CT TTTA ATG AAC ACCC TTCACTG GG TAG T AGCTCCT A GAGACTGC GCAAC DIA AGGAA TTTGT T CAA CT TCCC ATGAT GC G GAT AT CAACAATTA TACCC TA ecMHE R P G S Q A L P AVL DE F VG AVE M P neV R uECSE)AE AGRG L WAL VVQRMG R E G P CNL E L AD NFIqIQT eDR Q DA RW GE T F KRP M RI4 L N DSILIAQ AIIMGRG L s).K E Y VRDK1 D:F VGINARIA F P DKKL KKP E TGGKSY dO L K i DTP QE O SE R RE GF HE NF D L GF RHDYL E PEISRDI. cNA P CWE TLNLSITGN RQDIAL R YNKL N HGSAVY HYSE yaD tioIRVT D D viniDMLIDKAINNWQRNIF D DG KL L QTG T E GV Q P GRRP L F P Q F L ADSKE G P DGKVAITIDAILITKWP tcmECIK AS(MVWAVE AQAFGIK D P T E HS(M G A W TVTGD P V D GL E DAY P M HIP F K P L YVEDIM P E G R G atseh gt 2 3iorH H hpi2 2 n 6 6 h 4 4 tiU Q Q wsC Deae:a2l ielenalain i oleio elcbr sm u bsm b a oelueelueS n n T K p K p P A G T A G T M GIIL K M 4 H264 Q alleisb elK GTAAAATGC GTCGC GTAA GAGGGCCTGATGATGACCAC TGTCCA CTA G CCCGTCCCGTC GAGGG TC T A CGGG GT C G GGAG GCTCCC GCCGACAG CCCTGTT CGAGGTA C GTCATCT C CGCCCT CAT C GCT CCTGA TTA TA GTCAAA GG CGCTGATTC ACA TC G G T A A C GGT A C C GCC CGCCG CCGCTT CAGGACGACAA)ACCGA 9 GCCAAAC TGCCCTG CTCA 1 GGCAGGCAG GGGACA AGG:GGAA GGT GCCTCGCA C CA O GAAAG TCGGACGGAAGA GGCANCCACCGACCGCGAATTTGA D C T AT GA GGCC GC GCTT CGAGGCTCAGTIATGGCTCTCG A CGGGACTAGACAQ CCTGGCAACTGAGGGTGTCAAE C G G G C G G C C T G G G G G C C G A C GS(V S L L AACVL AY L T H Q TWDPV I L VL Y G L AR TN E P VTAPVIG E KMP W RNMVIR E E SMA P L MEHGYGE P H I S E L P R)F DG NA KHIVTKEI61 DT TA RTDR L TIE:SMDHQO L K AFRIV L SGVL A Y P VD ANAAAGAD VDF D QWASL AMGTL Q E ME GEIL K VSITA P F Q L S E TKRRP R A SHQTE A M R A M G V L N D RS(eaino m uen p Example 3. Identification of Acetyl Transferase Acetyl transferases (AcTs) capable of converting phenol to phenyl acetate in S. cerevisiae were identified. Each of the engineered S. cerevisiae strains containing four copies of various AcTs (500 distinct AcTs were tested) was cultured in minimal media. The AcTs in each strain were expressed via galactose induction and the assay was carried out by substrate (phenol) feeding at the given concentration (500 mg / L) for 24h. The strains that showed phenyl acetate production were shown in FIG.3. The sequences of AcTs with highest activity are shown in Table 3 below.

[0003] ).C TTGTCGA TTTGTCA GCCGA GGGTGTTA TCA TGTTTAAGTCATTG ATG O CAT CTTGTCTAAATCT CGTTCCT C N GAATT ATCCATC CTCT CA CGAAGAGT A A A ACCTTA A ACGGAT GAATAAG D AGGGATCAA AG ATGACTTAA TGGT I A C Q CGCTATC GTA AGA GCAAATT TAT A GCAT GC CAAAC GTTATAAAG GG TAAAAACTAA TTAAACGAGCCCTGG E AGGGGTCTCTAATC GT AACTTCTT S A CTACTTCTACG ATAGACTTA TAAAA cn Q e VGNAWHL KPIT KCNK RMSIGGME P MRL R TP V VF THGTRPL E DKLIVIIE GWAIE G KPIYDVQIAL QGL u .qeARYTP R E TE SIL F GTQIMF E RQF KS)L L L SGE P NQL K HFIE HN N VE 1 ysQR Q YS tidiNANVILLIT TL M CN YSVNL DQ L YP SVSS RSIYF D GCF Q GNQS:vi cKHQD Y RHE KQL KKCIHE DP F E RRDKIVT F L MWHL L MGF T O SGPNtcao).E GR D NTL SL L ND CL SE MFIRS E F L D TN E PEIG WW TL HVVA L CVG L D niOIN EQL YTRQ L VKWVR L Y KDIHKA E DF KCF D P L KN DSDVV GNLIat IA P Y AASFID VNEIVDIWHICIL Q s mNN e MVDSNYVSTP FFIKYVA NDF F L L K E Y L K N Y Y G K F Y EIH P KNL S A ADIM ESIH F D Q L L P L G N K V T YS F T S KS(h gih e hni / t sea)hcyrt8 s 01 F tim(e54T 0A ws eora c aisi 2 ()cTrhvC c ucoceC8 S arT8 SecA2 A S : 3 8 elni7 a 9 br3 at9 T SDI1t8 TT GTGATT TACTA A AG A A CGCGTA CCTT TGTC CTTTC CACGG T CAG CTG TGTTT CACGC ACGAAAC TGA TC AIQL F VVE HTA L DS F LIIV E P L L S M P D QVNA NQIT DHKKV RDNL Q H CSPGGA L N KLYI IR AP DMLP F QNE GASSC V S KV E NL HF FKIREIL G F SL F E P VL S L RLF Y KGIYVFIP E F P QV GL DG D T L P A E T S G olemsim ucu C 38939 1t0 ACTTT T C ACT AA GAGC G TT A T C CCC GTA CG A CA CTCCT TTGGTCA GGG A C GATCG ATTCGT CCGT TA CTGTAAAGA AT AAG T TAT TTA CT C ATGT A SSIL GK R KQVE AGGITNMV L E P L AK T KPIKIRP MAV M F AA TGF P Q DQSSF P QDITKVL GP P KK)VFTIRMD P S2 VF CL KSVIL L SFIV CL VA:QF D HAIRADDMAF CQS L L O DL QL TL P KS SQ NR VV TM SIY NV GV EDIH KAL L ATD MVA YSFSWL AHQIY R VKIG GTV Q HSP V L WCAG G YVF RGNME R N T V L NL P E V DTIK AH SS( AC GC GGGCA ACG TATGT TCTGAC ACGTTATTCATG TT T CAA AC GAG TGA GAGA CTC CTTCTCCCA T TAGTATGACC GTTT TG CCG C TCG CCTTAT L D E P SQVIR E DQATN F SYRKGARGAQRKHAP TF R NAE TNSIFIP GP F DF L F MQHHNSGSAYE RAVL VTNSDDP QP RAD HSL E NE CGYGAPIAL TYD S L L STRNGRS L L NQNIC AP SDL E CV L FAIDNQFEE I G GDP D V F TIKF DTCGM SP YV DAMLIE ANL L TD L E Q NDH QHSG QK KYAR L GGQ GQIP HVRP QMV RDL GA V TP SHVDGTVHKVYLP RADR VVGG F VHP D VVMF CAGIP P ATNP F L Q YGN VYGQE ASGL DMARSASKWD C AL HL SP L TVVL L SVRAISL VGQDQ RS P P L ADE L NE AP L P N YE VDQP E A S Y AVF TR L SA AE AYIL RVRL RSKGP L GP CRL TL V L Y L DN AS DP S VS HQQTL HVL VQ F L AKL L AYV YE N L S V YS CIA G E W P A WR Y VIH L GMIR G Q A H Y V V S S A D G L A S Y Q C E D R W D N L N N T anitnarim a ecna hca L 97939 1t0 AAC ATT ACCACTTAGC T CGGA AATGTAGTGT TGTTAT TAAC ATTTCGATGGCAG AGA A AGA ACCTTGTTTCAGATGTTGCCT CTGAGT A GAC G T C E VASR HSF L W G R )QINA L T 3:P MRTP TRYL L O HRL QVIN KAKE Q H D E H KL ISIGRTL Q KNNC L T F RE DQSIYP ADN

[0004] L(M M A N K - HS nB sieacrC / )yts7tsm(1 al3aeoroc3.Y(ahir2)4 ccoS4 ab A6 Sra / 601 38939 1t2 C TGA A AATT CCCAATGTT TA CCGCTC ATTT TC TGACAG TA TTT T AAACCCCAATA TAACCT TTACGT TAAG A G C CGAA TAAT TTT GA A C ATTCG A T CAGATA TATAT P L N D PSA W VPIP RE RKCI ICG F TK DGNSIKE SNL R K GTLPIWA G E GME P VF TY AIE L E DKL FIGKPYMMQIGIS QGE QGIQL KEQIRNE AQ L SD TAE S YLLITP NYYSTIH VFIYF NNRNF K VL)4 TL M CNDP AF VN E L ADM Y DF Q NE:YK QLCIHL RP SVA VTQSIHG L CMGF TQS O E L S KKL NE E R E L L DKIF F RWAIGMGASGNSE QMIFIRSD RY RSKWWVSL NAVL CVP D L L AKWVL QDINKTCE E TF P TKNDVVS LIYVSATFIDFIVYIERIVF E DWQ SRIGNL Q YS YTP F HYNF MAHNDDSE VF KIL L SL KL E

[0005] N V E Y G K F DEIG E Q L P P F K KNIT YS F T AS( T AG AACTCTA AGTG GTC TAT G G A GCTCAT G A TCG C GTTAACATGAGAC TT TG AAATG CATG C T G A GTT A AGTG T GAT CAATAGCAAT ATCC CC TT E E TR E N P P DVSL WP NSYTRP KKTS CPTIF F S QSF ARR N PLIAPIDGT D RPIVSIT R K VGNL L RAAQVF TDCKIL L F L GNC C GD SM P S RYL L GE L E N E AE M QYKIIKWA TRL QVIYDLTP CN L YP SSE G TPKPIKSKD Y HE LITL KQL HE DP RFVIIF NH ESHQKL SL KKCIN K R L V SDE F L E ST YGRTL SE TN T P MFL RDID NC LIRV Y HDKIVT QL YP YL L KWFIL DE MSSKF L NIADNY N K KVAA FFINYS N T P K F Y EIKTWW M M A T Q FEIR C E )tsseaceyY(m osru an hacyca ab Sue97939 1t6 CCGT GCA C G AG C CTGGTTTT CT TG G TGTGC GG ATA GTTG A GA ACT TATT ATAT TAT ATTCCAGCACA GT T G TGCCAATAT TATAAAGACT TA E THLIA E WNC E S SGML E GE)QQ L 5 HF K:F QVL O MGNE TQPNGF VASS D SGN LINL SDVVL Q V E LRIG L L N AS( AACTTT AA ATTAGG TGTCTAAGGTGGTTA T GAGCAAA CCA T GAAGT A ATA TATAACA G TACCATATTACATTAG ATA A C ATGAAT A TAACAA T CACA L NQEISD L RGIGQ E AL L QF E L HF YVP TTS RWGF YL TYKIF GL YV L L L STSNDA RF Y VHDEP KKTSG S DAKAQCYE A E SHDINFITSL E TIA HNYKP HQF DP EF VKRP F NAAE L DYWD S NIIL CTGI )P E VL YQP NDNGGE DEDKNARIQIL NHSF GKAD RVGT6 E L TVH KF NKG L DSIKYYC QF S HNE P P GKNNGVNQ L Q:HF L P TG DDIS KL DDE VYO Y PMIKP CIE SVTTF G GYGV GGNSMIIKSL FIIDCFIRYP QL F RVNYSVIRYF SF LNEIM RYL T Q L DQ E VKH G L V QDIF SKTL RND GE F QP AMKDIDRMRHYDSP ISP NL T DTITYTC GKAS GE L DQKF DCQ E AKKA L E FIL A VLEP TRSF DD L N F L HTR YPIR L TL MF E N TE E KL S L E E Y DIA Q S M H QCIF K P L F T H H RS P K D D L Y D A N ES(sniea / scyrt8'rs m(05eka oe4 r a ai0B(hsi 2cvC)c )cerC88tsa T A2a SecSey68939 1t6elbaCGAGT TTGT TGAG T TG ATC ACCAT CTTACATC TATn TACTC AG TTAG ACGA AT TTT CTTTCAACGGGCi A C TA C AGTTTG CAGTTT ACTGAC AAC C CTCA TTTteieT TACTC T CCCGC TC T A A TAAAGGT AA AACA T)cadeneTACT AAGTAGA G TTCTAT CA 6 TGTGT T TCA CTGAC C2lssg GGATeT G ATTTATAGAG G T C AT:y GTA ATCCT CTGGn erh TTGACTAACT CTGT GAG TATATAC G AT C TCO Nep h xtllTT A CATATC TC ACTAAAT TAAGAC TTCGACATTTTDp e-aCCTGAAACGTGTCTTTTACGCAI egreg TTGCTCTATCATATTGCTCATTQsn TACAGCGATTACTCAATGGAGGE

[0006] T A C A A T G T T T C C T G G A G C T C G CS(ocicvoniuluessegd orre rp m pwx or rtae- f o etfht rev tyo aaya lecwh whleatlat cypatsec po nisihhteh pfhtt An n.)oy isn nsoi en wo oitbec aghstuds ralon orm Parucgit ata.a rad 4idp (els dep B1et.di cma vuxG orrtsEIFpn 4 o elcsbaaTw4 5sihtd G naA CG A G T C T GA C T G G G TT G CT T CT , T G C T CT G A GC A G A A A A C T G GC T GG C GA d G AC T G GA CT A T T CC A A GT G T TA T AG e G T CG A A C A t GG G C T G G TG C A TA C G GA A AT c A C TA C C u A G GC G A CT T T A CT G CA C G C T G G T A C T C r T A AT T G A GA A G A G A A G A TT C t G GC C s A T A C CA C AG A GC C C GT G G C GT A CA n G T CA G C T T TC A AA C TA A T G TT T AT G GA o T T TG A A GA G GC T AA T T CA A AG C T A TC c T T CG A G GT A A CC G CC C T CG T GG A AC sa ec A A AT A G CC A CG G CA T A T TT T C TC T TA C A AA C T AG G TT A G T T T A G CC A AA G CA wneA G C CT T C AT T A TA T T GG T G TC C T CA C GT G GA A A T T T CC T GC nud(ss cSG D T P MS GGAGL AWATL Q P DLIYL VL KRSIS bee neV QL YP Q L HGGKT P TE QAQWGGVWIus ta rp u llteqAHSVGTGAF G e L GWF TRL L VADIYAIA MGNF KSGSN F SDYRSNF V TY NP acaxesKS RL S r d NL P N DH iDIAV G RL L GAYLTAGKTQTSIE AIHGQL L KMSKYL L VF Y SKHKR VL NILF H RADNGATG gl e cDKH QT YANRDTP HSDNATE SSGGS niy vadneofo).TSANIMS ANE DKE SK W YL P GMGL niO F QVA RF VMDSDANKGL YKL TVTS A TP WY E ASSID QV E N P TL SAYP S ulh o mNTDADL QV LYIVGKA E AL E DP H L cpsDiIP L KGMTGADNSHKQNGKSAP E KR n A M V M N A L P G F EIE E L L V P A L S L S Q R Y V ,.L / ecg.gne(meu e3 qesaidnsen u dcoomrnya m oera ueadni ec aihsivnepcg uirrucocerS a Seacld leorO:isp 4bniel e1 L elabneK Krtsa T G T T G GA A GG A T G C TA T AA T CT T A GC TA T A A T A A C A T T A A AG T CT C TT T C A C CG T A T GC GA T CG A T AT T G C CC G AG T A EDP K:VITD SGF GO MIFSGF KNP QF YD KFIVHFAIQ NAVTE DP Y S KEP K(L QF VGAAA SWKRK L C G E K C A CA T GT T CT G GC C T T T T C A G T G C T AT GG C C A A TC T C A C T TT T G T AG A C A CG AT A A C A CG C G GG A TG G A T AC G A TT T A GT NG TL VVVAL K W FSTD ADSP AARKVE A VVVDIDPIAF VANVNGEIRE GTV ALKIP KGE KML)VTDIE P V TE L E QRD TD YASGAT 0 QVTL QVIAK KVS QSKVGAGL NADVI3:KTDKE KTVAFSVE GYNME E ND O QGQAE TLIDGAF FP KKKIL KL ASNASP Y E TT F EQILSIYKE KKDF D P AQP KKSQ L Y GL GTL D DDASF KIE KF QGF REF E L TKYTL L VRRIAQ SL KKHE AL NS F E A WNVGYRAP KGT M QIA K V D K T C Q TIF P D S E VS(secym oera aihsicvcaerSec1 L A T A C C AA A G G AA A AC A A AC TA T TT T A C AC T C T TC C AG G A A CA C A CT C T T A CA G A A A TT A C A C CC C TC T G C A T A G GA G AT T TC G D TISGT L AE SWG D ALP SAA L GGA A DVVVM I P GE L F M VP L HP VFIDSVVGL E SF D N MAP G NADHVIE TD DRG AL DRGP SQIS NASI ISSAT MG RF HTHQSP RR L K CAP SNL T P VY G TYRRN AL K RP L KG Q L Q QSNAQNL YG DQSGAE D F E P E KAL P G L AADD KEP DCK ML STF K QTAIVF YHL T AAKQKIVRVP L NP RG VRVGE NSQ M M Q L R R D K D A P M Q G M N A ilo caih cireh csE F orA T C G T C G T AA T GT A C GG T T T A GA C G T A AT C CC C T A C AA T A T G A GG G TA T GC G T A AC T C G TG T A TG T A C A T G A A G C GG A T TA C KAA P SLLINL G M V Y VTG QK Y E D SKY F GRS C STR)3 RL S L G P L DVL Q DKIRMA T3 E L P VTAYL L TP L DV P E L:GF A D L NL VS ATHVE QWQO L S L P A E T TVVTA NV SSIGNL SCND VAP E NGATAV QALI VIE TALSDFQV I AVSGS ND DQ RNVQKRGF T RKAP A TQE E F E L L L YGT L VGQL GSH E

[0007] E V H(M G M V Q P D G G Y R ilo caih cireh csE B orA G T T T AT C A T CG G T TT T CA A TT TC T TC C T TT T C GT T TA A G A G A A A T G C G CT C AT CA T T C A G T C G TC A T GA A G T A A TG C CC G GT G L L KNWT YR G L NRL A E TE HR S AL E L GAL MH DLIDCAYATQ I AE S)GIKVK L CRGIG MRS V 6 VVRA A 3 L S NRL M G:AWA E MVQ L S DIE A ERIG L CTE MTE E AGE RVRAO S KDLIAP KV E QNV M TKDV WYREAEIASGKSCDIVAF S N AASND MDE F MD VF RKDQ T F AH AQVP LGIAIE KLSAV E

[0008] AA P AG F E G L M A AS(M V RN S ilo caih cireh csE D orA T A A G TG A TG A C A TA A AT C A AA T C C AG A GT C AC T A T T G A GA G C CT A TG G G CA G GA T C T G A AG G TA T C TG C A G A C A C T AA A C T AT A G S SD L T S EDIV K AA RL T TAL SQ L L L E E SRA KAQMR V SYRAH)V AL SLP GP SRP AAD L RQQSIKLI9 R D WVL GTF GL SRDV AP E 3 VKT:L DTE AS F CL L W RNGK F L V MQ L KE L L TIIGV O QL L TY E T F DE L MTAVNTL GPILSRGT FAIL HEAIE KGT L D QQEIE VGAL L YE AAKL TAF R LIAP P QNRP L DL LP AL KEDIHEPPIAMTDQ HDEF QL VP TRLP ATD SANE SL RE WVKGIK

[0009] E T A S M Y K A L MA S VS(MA P KV T F Y R GEIG ilo caih cireh csE LP C C A C T T GT T T A T G GC T T G A C T T G T T T T A TT G GNT A A TA T D G A C TG T C CTIC G C CA A AA Q C A A AG G GT E A C C C A A T GS(GAAT T GTA GCGAG CTAAGCTTC CGAT CCGC CCC GCAGCTGG TA TACCCA C TAA AGCTT CCTAATCGG GTTG GTGCT TCTCC GGG TGG TTCA TAC G CGGC GG CTGTAGCCC C CCG TG CGAAA G A ACCCCTCAT T TA AT ATGG GTT G TGACAGGGT)CGACA T GGT 3 GTGA G G A GCG 4 TGCA T CTGGTA:CCA O ACGTAATAC G AANG CT A T GA GTTTTACD CTGGTTCTGAICGCGGCGAATQ GCGTTAGGCGE T T A T C G G C A TS()24:O N DIQ E S( Example 5. Construction of a Saccharomyces cerevisiae that Produces Phenyl Acetate (PA). Several S. cerevisiae strains were engineered using the 4-HB DC and AcTs described above in various combinations. Each of the engineered S. cerevisiae strains containing four copies of the 4-HB DC (e.g., 4 copies of each of the subunits) and four copies of various AcTs (>1004-HB DC and AcT containing strains) was cultured in minimal media. The DC and AcTs in each strain were expressed via galactose induction for 24h, followed by substrate (4-HB) feeding at the given concentration (500 mg / L) for additional 24h. In addition, those strains were engineered to knock out two endogenous enzymes [SAY1 gene (P53324 - Steryl acetyl hydrolase 1) and IAH1 gene (P41734 - Isoamyl acetate-hydrolyzing esterase)] that are believed to be involved in undesirable hydrolysis of phenyl acetate in S. cerevisiae. Various strains that showed phenyl acetate production are shown in FIG. 4. Strains 2157636.00, 2157637.00 and 2157635.00 are biological replicates; each comprises ATF1 [AcT from Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Uniprot accession number: P40353, Alcohol O-acetyltransferase 1] and DC from Klebsiella pneumoniae (e.g., all subunits of this enzyme), and a knockout of IAH1; these produced about 2 to over 4 mg / L of phenyl acetate, as shown in FIG. 4. Additional strains were constructed which comprise ATF1 and DC from Klebsiella pneumoniae (e.g., all subunits of this enzyme), and a knockout of a different esterase, but these did not produce significant amounts of phenyl acetate, as shown in FIG. 4. Acontrol strain designated by the symbol in FIG 4. comprised ATF1 only, withoutDC, and without any knockouts of any esterases. The assay with this strain was performed by feeding phenol as the substrate, to make phenyl acetate in this control. For the other strains whose data is provided in FIG. 4, 4-HB was used as the substrate. Additional strains were constructed comprising DC from Klebsiella pneumoniae (e.g., all subunits of this enzyme) and AcT from Cucumis melo, with double knockouts of both SAY1 and IAH1; these produced around 7 mg / L phenyl acetate (data not shown). Additional strains were constructed comprising DC from Klebsiella pneumoniae (e.g., all subunits of this enzyme) and AcT from one of: L. mirantina, S. arboricola, S. eubayanus, or S. cerevisiae ATCC 204508 / S288c; each of these strains also comprised a single knockout of IAH1 or SAY1, or a double knockout of both SAY1 and IAH1. These various strains produced between 0.5 and 5 mg / L phenyl acetate (data not shown). EQUIVALENTS Those skilled in the art will recognize, or be able to ascertain using no more than routine experimentation, many equivalents to the specific embodiments of the invention described in this application. Such equivalents are intended to be encompassed by the following claims.

Claims

CLAIMS What is claimed is:

1. A host cell comprising a heterologous polynucleotide encoding an acetyl transferase (AcT) wherein the host cell is capable of converting phenol to phenyl acetate.

2. A host cell comprising a heterologous polynucleotide encoding a 4-hydroxybenzoate decarboxylase (4-HB DC) wherein the host cell is capable of converting 4-hydroxybenzoate to phenol, wherein the host cell is not a bacterial cell.

3. A host cell comprising one or more heterologous polynucleotides collectively encoding: (i) a 4-hydroxybenzoate decarboxylase (4-HB DC); and (ii) an acetyl transferase (AcT), wherein the host cell is capable of converting hydroxybenzoate to phenol and of converting phenol to phenyl acetate.

4. The host cell of any one of claims 1-3, wherein the host cell is a yeast cell.

5. The host cell of claim 4, wherein the yeast cell is a Saccharomyces cell.

6. The host cell of claim 5, wherein the Saccharomyces cell is Saccharomyces cerevisiae cell.

7. The host cell of claim 1 or claim 3, wherein the host cell is a bacterial cell.

8. The host cell of claim 7, wherein the bacterial cell is an E. coli cell.

9. The host cell of any one of claims 1-8, wherein the host cell comprises a heterologous polynucleotide encoding an AcT, wherein the AcT comprises a sequence that is at least 90% identical to any one of SEQ ID NOs: 1-6.

10. The host cell of claim 9, wherein the AcT comprises the sequence of any one of SEQ ID NOs: 1-6.

11. The host cell of claim 9 or claim 10, wherein the AcT is a benzoyl transferase.

12. The host cell of any one of claims 9-11, wherein the host cell comprises at least two, at least three or at least four copies of the heterologous polynucleotide encoding AcT.

13. The host cell of any one of claims 9-12, wherein the host cell comprises one or more polynucleotides collectively encoding two or more of: an AcT having a sequence that is at least 90% identical to SEQ ID NO: 1; an AcT having a sequence that is at least 90% identical to SEQ ID NO: 2; an AcT having a sequence that is at least 90% identical to SEQ ID NO: 3; an AcT having a sequence that is at least 90% identical to SEQ ID NO: 4; an AcT having a sequence that is at least 90% identical to SEQ ID NO: 5; and an AcT having a sequence that is at least 90% identical to SEQ ID NO:

6.

14. The host cell of any one of claims 1-13, wherein the host cell comprises a heterologous polynucleotide encoding a 4-hydroxybenzoate decarboxylase (4-HB DC), wherein the 4-HB DC comprises a sequence that is at least 90% identical to any one of SEQ ID NOs: 14-16.

15. The host cell of claim 14, wherein the 4-HB DC comprises the sequence of any one of SEQ ID NOs: 14-16.

16. The host cell of claim 14 or claim 15, wherein the host cell comprises at least two, at least three or at least four copies of the heterologous polynucleotide encoding 4-HB DC.

17. The host cell of any one of claims 14-16, wherein the host cell comprises one or more polynucleotides collectively encoding two or more of: a 4-HB DC having a sequence that is at least 90% identical to SEQ ID NO: 14; a 4-HB DC having a sequence that is at least 90% identical to SEQ ID NO: 15; and a 4-HB DC having a sequence that is at least 90% identical to SEQ ID NO:

16.

18. The host cell of any one of claims 1-17, wherein the host cell comprises at least one heterologous polynucleotide encoding a 4-hydroxybenzoate decarboxylase (4-HB DC) capable of converting 4-hydroxybenzoate to phenol, wherein the 4-HB DC comprises a sequence that isat least 90% identical to any one of SEQ ID NOs: 14-16; and at least one heterologous polynucleotide encoding an acetyl transferase (AcT) capable of converting phenol to acetate, wherein the AcT comprises a sequence that is at least 90% identical to any one of SEQ ID NOs: 1-6.

19. The host cell of claim 18, wherein the host cell comprises one or more polynucleotides collectively encoding: a) two or more of: a 4-HB DC having a sequence that is at least 90% identical to SEQ ID NO: 14; a 4-HB DC having a sequence that is at least 90% identical to SEQ ID NO: 15; and a 4-HB DC having a sequence that is at least 90% identical to SEQ ID NO: 16; and b) two or more of: an AcT having a sequence that is at least 90% identical to SEQ ID NO: 1; an AcT having a sequence that is at least 90% identical to SEQ ID NO: 2; an AcT having a sequence that is at least 90% identical to SEQ ID NO: 3; an AcT having a sequence that is at least 90% identical to SEQ ID NO: 4; an AcT having a sequence that is at least 90% identical to SEQ ID NO: 5; and an AcT having a sequence that is at least 90% identical to SEQ ID NO:

6.

20. The host cell of any one of claims 1-19, wherein the host cell comprises one or more genetic modifications that result in decreased expression, relative to a control host cell lacking the one or more genetic modifications, of at least one endogenous gene encoding an esterase.

21. The host cell of claim 20, wherein the host cell has decreased expression of SAY1 and / or IAH1, relative to a control host cell lacking the decrease in the expression of SAY1 and / or IAH1.

22. The host cell of claim 20 or claim 21, wherein the one or more genetic modifications comprise a knockout of an endogenous gene encoding an esterase.

23. The host cell of claim 22, wherein the one or more genetic modifications comprise: a knockout of SAY1 and / or a knockout of IAH1.

24. The host cell of any one of claims 20-23, wherein the host cell produces more phenyl acetate compared to a control host cell that does not comprise the one or more genetic modifications that result in decreased expression of at least one endogenous gene encoding an esterase.

25. A method for producing phenyl acetate, the method comprising culturing the host cell of any one of claims 1-24.

26. The method of claim 25, further comprising isolating phenyl acetate from the cell culture.

27. The method of claim 25 or claim 26, wherein the cell is cultured at pH of about 6 or below.

28. The host cell of any one of claims 1-24, wherein the host cell further comprises one or more copies of a polynucleotide encoding one or more glycolytic enzymes, PPP enzymes or a combination of one or more glycolytic enzymes and PPP enzymes.

29. The host cell of any one of claims 1-24, wherein the host cell further comprises one or more copies of a polynucleotide encoding a DAHP synthase.

Images