18 results about "Acyl coenzyme" patented technology

The invention discloses an acyl-coenzyme A oxidase mutant as well as an expression strain and application thereof. On the basis of acyl coenzyme A oxidase derived from marine microorganisms, mutation sites are designed through Saprot and scored, and mutation is introduced through overlapping extension PCR (polymerase chain reaction), so that a mutant gene is obtained. After the engineering bacteria containing the mutant plasmids are subjected to induced expression, the acyl-coenzyme A oxidase with improved stability and specific enzyme activity is obtained. Under the condition of 37 DEG C, the stability of the mutant is improved by 1.3 times. When palmitoyl coenzyme A is used as a substrate, the specific enzyme activity of the mutant is improved to 1.5 times. The mutant has application value in an in-vitro diagnostic kit for detecting free fatty acid by an enzyme method.

The invention provides a genetic engineering strain of high-yield immunosuppressant mycophenolic acid as well as a preparation method and application of the genetic engineering strain. The invention firstly provides a method for constructing the penicillium with the effect of high yield of mycophenolic acid. The method comprises the step of replacing an indigenous promoter of acyl-coenzyme A oxidase PbACOX323 protein participating in beta oxidation in peroxisome of a penicillium strain with a promoter PgpdA of 3-phosphoglycerol dehydrogenase with an amino acid sequence of SEQ ID NO: 1. According to the method disclosed by the invention, the genetically engineered bacterium with high yield of mycophenolic acid is constructed, the yield of mycophenolic acid is positively increased by replacing a promoter of acyl-coenzyme A oxidase PbACOX323, and the method has a good industrial application value.

The invention provides soybean acyl-coenzyme A oxidase and application of a coding gene thereof in regulation and control of plant salt tolerance, and belongs to the technical field of plant breeding. The invention provides soybean acyl coenzyme A oxidase and a coding gene thereof. Experiments prove that the soybean acyl coenzyme A oxidase or the coding gene thereof can improve the salt tolerance of plants through positive regulation. Therefore, the invention provides the application of a reagent for improving soybean acyl-coenzyme A oxidase or gene expression or activity or a reagent for increasing or enhancing gene expression in increasing the salt tolerance of plants, preparing a product for increasing the salt tolerance of plants, cultivating plant varieties with salt tolerance advantages, preparing a product for cultivating plants with increased salt tolerance and breeding plants with salt tolerance.

The invention provides an acyl coenzyme A transferase mutant and an application of the acyl coenzyme A transferase mutant in synthesis of 3-aminopropanol. The acyl coenzyme A transferase mutant comprises: 1) a protein having an amino acid sequence E249 mutated at the following sites of SEQ ID NO: 1 and having acyl coenzyme A transferase activity; and 2) protein which has an amino acid sequence with homology of at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% with the protein in 1) and has acyl coenzyme A transferase activity. The acyl-coenzyme A transferase mutant can be used for synthesizing 3-aminopropanol by taking beta-alanine as a substrate, so that the vacancy that the current market is lack of a biosynthesis method for synthesizing 3-aminopropanol is made up, and the acyl-coenzyme A transferase mutant has the advantages of greenness, environmental protection, simplicity, convenience and the like, and is wide in application prospect.

The present invention relates to a recombinant yeast for high-level production of adipic acid, wherein the activity of endogenous acyl-CoA oxidase is weakened compared to the inherent activity, and the activity of plant-derived acyl-CoA oxidase is enhanced compared to the inherent activity. The recombinant yeast according to the present invention can produce adipic acid at a high yield compared to existing unmodified microorganisms.

The present invention discloses a genetically engineered Schizochytrium strain for efficient DHA production, as well as a construction method and application. The genetically engineered strain is obtained by knocking out the peroxisome matrix protein gene PEX10 in the wild-type Schizochytrium, which disrupts the β-oxidation pathway and blocks the degradation of fatty acyl-CoA; overexpressing the acetyl-CoA carboxylase gene ACC1 to provide more malonyl-CoA precursors, thereby promoting fatty acid biosynthesis; and overexpressing the diacylglycerol acyltransferase gene DGAT to promote the accumulation of fatty acids in the form of triglycerides. Under shake flask conditions, after fermentation, the DHA and PUFA produced reached 55.10% and 70.47% of the total oil content, respectively. Compared with the wild-type strain, DHA and PUFA increased by 21.6% and 24.77%, respectively, without a significant change in biomass, showing extremely high application potential.

The present disclosure relates to synthetic biology and, in particular the bioproduction of isoprenoids using heterologous expression of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase (HMGR) enzyme(s).

Disclosed herein are novel cells that are engineered to catabolize a reduced number of acyl-CoA and branched-chain amino acids, and methods for improved cannabinoid production using these cells.In addition, disclosed are cells that are engineered to produce rare cannabinoids, methods for producing these novel rare cannabinoids, and the novel rare cannabinoid compounds thus produced.Some aspects of the disclosure are directed to cells that are engineered to provide increased production of cannabinoids and / or their derivatives compared to control cells.

The invention relates to the technical field of biology, in particular to an enzyme related to synthesis of kaempferol-3-O-(2 '-coumaroyl)-glucoside, a coding gene and application of the enzyme, and discloses acyltransferase CsCFAT, the amino acid sequence of which is shown as SEQ ID NO.1. The acyltransferase CsCFAT effectively solves the problem that existing kaempferol-3-O-(2'-coumaroyl)-glucoside is difficult to obtain. The invention discovers and identifies that the acyltransferase CsCFAT has the function of catalyzing kaempferol-3-O-glucoside and p-coumaroyl-coenzyme A to generate a target product for the first time, and fills the blank of a specific biological catalysis tool of the compound; compared with traditional plant extraction and chemical synthesis, large-scale production of CsCFAT is achieved through prokaryotic expression, a recombinant protein band after purification is single, a single product peak can be generated through catalytic reaction, and the obtaining efficiency and purity of a target compound are greatly improved.

The application discloses a preparation method and application of acyl-CoA oxidase. In the application, a strain source capable of expressing soluble acyl-CoA oxidase with high enzyme activity is screened from a large number of acyl-CoA oxidase-containing strain sources through genetic engineering technology, and a corresponding industrial production method of acyl-CoA oxidase is provided. The method has simple purification steps, high enzyme activity, high protein expression amount and low production cost.

Target RNA molecules are labeled through biotin, and accurate tracking and efficient detection of RNA can be achieved. The ribozyme capable of transferring biotin acyl to the 5'terminal of RNA (Ribose Nucleic Acid) is obtained by screening by utilizing an in-vitro screening technology and taking small molecule 12: 0 biotin acyl coenzyme A as a substrate. Then, a conservative motif of the ribozyme is obtained through screening optimization, and a biotin modification site of the ribozyme is determined. The ribozyme is designed into enzyme chain RNA with trans-activity, the biotin modification activity of the ribozyme to substrate chain RNA is verified through EMSA, urea denatured polyacrylamide gel electrophoresis and mass spectrum identification methods, and meanwhile, the transfer site and the molecular weight are determined. The ribozyme obtained by the invention can efficiently and specifically carry out biotin labeling on target RNA, the reaction process is simple, and the labeling activity is up to 90% or above.

Disclosed herein is a method for predicting prognosis of a subject being with a cancer, such as a malignant glioma, being treated with an oncolytic herpes simplex virus (oHSV) that involves assaying a sample from the subject for Acyl-CoA-binding protein (ACBP) levels, wherein an elevated level of ACBP compared to a control is an indication of a poor prognosis. Also disclosed herein is a method for treating a cancer, such as a malignant glioma, in a subject that involves administering to the subject an effective amount of an oncolytic herpes simplex virus (oHSV) in combination with a glioma Bmi1 inhibitor or a fatty acid oxidation (FAO) inhibitor optionally followed by one or more immune checkpoint inhibitors.

The invention provides engineering modified saccharopolyspora spinosa and a method for producing spinosad by using the engineering modified saccharopolyspora spinosa. The saccharopolyspora spinosa overexpresses g6pdh-1. The content of NADPH (nicotinamide adenine dinucleotide phosphate) in the modified saccharopolyspora spinosa is increased, and the content of acyl coenzyme is increased, so that the synthesis of a lactone ring is improved, and finally, the increase of the yield of spinosad is realized. The transformed saccharopolyspora spinosa can greatly improve the yield of spinosad, and is of great significance to industrial production of spinosad.

The invention provides a genetically engineered bacterium, a construction method thereof and a method for synthesizing 3-aminopropanol. The genetically engineered bacterium comprises an acyl coenzyme A transferase gene ACT which is introduced from an external source, and the genetically engineered bacterium further comprises an alcohol dehydrogenase gene adhE. The method for synthesizing the 3-aminopropanol through catalytic reaction by using the genetically engineered bacteria and taking the beta-alanine as the substrate overcomes the problem that the existing method is lack of a method for converting the beta-alanine into the 3-aminopropanol through a biological fermentation method by taking the beta-alanine as the substrate, and lays a foundation for large-scale production of the 3-aminopropanol; and a new thought is provided for a path for further synthesizing other chemical substances based on a biotransformation method.

A use of a substance for inhibiting SOAT1 gene expression and / or protein activity. The use is selected from at least one of: (a) Preparation of kits for liver cancer diagnosis; (b) Preparation of kits for liver cancer prognosis; (c) Preparation of companion diagnostic kits for treatment of liver cancer; (d) For the preparation of drugs for the prevention and / or treatment of cancer; (e) For the preparation of drugs for the prevention and / treatment of cancer spread and metastasis; (f) For the preparation of drugs that promote the apoptosis of cancer cells; (g) For the preparation of drugs for inhibiting cancer cell formation; (h) For the preparation of drugs that inhibit the proliferation and growth of cancer cells in vitro. Experiments have shown that SOAT1 is highly expressed in liver cancer tissues and serum, and its high abundance indicates poor prognosis of liver cancer patients.

The application discloses a kind of recombinant halomonas producing polyhydroxyalkanoate and its construction method and application.The recombinant halomonas includes exogenous gene, the exogenous gene includes aldD Gene, dhaT Gene and orfz The combination of gene, and the recombinant halomonas weak expression endogenous prpc Gene.The application introduces the synthesis pathway from 1,4 butanediol (BDO) to 4-hydroxybutyryl coenzyme A by exogenous, successfully constructs P34HB synthesis pathway, can effectively regulate the proportion of each monomer in copolymer, especially after exogenous addition short-chain fatty acid (such as formic acid, acetic acid, propionic acid, butyric acid, etc.), can further improve the synthesis of PHB, PHBV, P34HB, P34HB3HV and other copolymers, and adjust the proportion of different monomers, enhance the diversity and yield of copolymer.

The invention discloses an acyl-coenzyme A carboxylase beta subunit mutant and application thereof in increasing the yield of glutamic acid, and belongs to the technical field of biology. The acyl coenzyme A carboxylase beta subunit mutant comprises a protein of which the amino acid sequence is as shown in SEQ ID NO.3. Experiments show that the point mutation accd5-3C878A gene or the overexpression accd5-3C878A gene of the accd5-3 gene coding region in the wild type ATCC13869 and the corynebacterium glutamicum CGMCC No.29950 are respectively beneficial to the increase of the yield of the L-glutamic acid.

The present invention relates to a method for the production of atactic poly(3-hydroxybutyrate) (PHB) comprising (a) producing a mixture of (R)-3-hydroxybutryl-CoA and (S)-3-hydroxybutryl-CoA by (a1) reducing acetoacetyl-CoA to a mixture of (R)-3-hydroxybutyryl-CoA and (S)-3-hydroxybutryl-CoA by contacting acetoacetyl-CoA with an enzyme catalyzing the reaction (R)-3-hydroxyacyl-CoA + NAD(P)+ = 3-oxoacyl-CoA + H+ + NAD(P)H and an enzyme catalyzing the reaction (3S)-3-hydroxybutyryl-CoA + NAD(P)+ = acetoacetyl-CoA + H+ + NAD(P)H in the presence of the coenzyme nicotinamide adenine dinucleotide phosphate (NADPH) or nicotinamide adenine dinucleotide (NADH), and / or (a2) the isomerization of (R)-3-hydroxybutyryl-CoA to (S)-3-hydroxybutyryl-CoA by contacting (R)-3- hydroxybutyryl-CoA with an enzyme catalyzing the isomerization of (R)-3-hydroxybutyryl-CoA to (S)-3-hydroxybutyryl-CoA, and / or (a3) the isomerization of (R)-3-hydroxybutyryl-CoA to (S)-3- hydroxybutyryl-CoA by contacting (R)-3-hydroxybutyryl-CoA with an enzyme catalyzing the reaction (3R)-3-hydroxybutyryl-CoA ↔ crotonyl-CoA + H2O to produce Crotonyl-CoA and contacting Crotonyl-CoA with an enzyme catalyzing the reversible hydration of crotonyl-CoA, and (b) polymerizing the mixture of (a) to atactic poly(3-hydroxybutyrate) by contacting the mixture of (a) with an enzyme catalyzing the reaction -3-hydroxybutyryl-CoA + poly(3-hydroxybutyrate)(n) = poly(3- hydroxybutyrate)(n+1) + CoA.