43 results about "Acyl Coenzyme A Synthetases" patented technology

Organisms are provided which express enzymes such as glycerol dehydratase, diol dehydratase, acyl-CoA transferase, acyl-CoA synthetase β-ketothiolase, acetoacetyl-CoA reductase, PHA synthase, glycerol-3-phosphate dehydrogenase and glycerol-3-phosphatase, which are useful for the production of PHAs. In some cases one or more of these genes are native to the host organism and the remainder are provided from transgenes. These organisms produce poly (3-hydroxyalkanoate) homopolymers or co-polymers incorporating 3-hydroxypropionate or 3-hydroxyvalerate monomers wherein the 3-hydroxypropionate and 3-hydroxyvalerate units are derived from the enzyme catalysed conversion of diols. Suitable diols that can be used include 1,2-propanediol, 1,3 propanediol and glycerol. Biochemical pathways for obtaining the glycerol from normal cellular metabolites are also described. The PHA polymers are readily recovered and industrially useful as polymers or as starting materials for a range of chemical intermediates including 1,3-propanediol, 3-hydroxypropionaldehyde, acrylics, malonic acid, esters and amines.

The present invention relates to a cell for producing acyl glycinateswherein the cell is genetically modified to comprise -at least a first genetic mutation that increases the expression relative to the wild type cell of an amino acid-N-acyl-transferase, -at least a second genetic mutation that increases the expression relative to the wild type cell of an acyl-CoA synthetase, and -at least a third genetic mutation that decreases the expression relative to the wild type cell of at least one enzyme selected from the group consisting of an enzyme of the glycine cleavage system, glycine hydroxymethyltransferase (GlyA) and threoninealdolase (LtaE).

The invention relates to methods for producing a wax ester in recombinant host cells engineered to express a thioesterase, an acyl-CoA synthetase, an alcohol-forming fatty acyl reductase, and a wax ester synthase. The methods of the invention may take place in photosynthetic microorganisms, and particularly in cyanobacteria. Isolated nucleotide molecules and vectors expressing the thioesterase, acyl-CoA synthetase, alcohol-forming fatty acyl reductase, and wax ester synthase, recombinant host cells expressing the thioesterase, acyl-CoA synthetase, alcohol-forming fatty acyl reductase, and wax ester synthase, and systems for producing a wax ester via a pathway using these four enzymes, are also provided.

The present invention relates to an acyl-CoA synthetase homolog protein from microorganisms of the genus Mortierella, a polynucleotide encoding the protein, and so on. The invention provides polynucleotides comprising an acyl-CoA synthetase homolog protein gene from, e.g., Mortierella alpina, expression vectors comprising these polynucleotides and transformants thereof, a method for producing lipids or fatty acids using the transformants, food products containing the lipids or fatty acids produced by the method, etc.

Cells and methods for producing polyhydroxyalkanoates. The cells comprise one or more recombinant genes selected from an R-specific enoyl-CoA hydratase gene, a PHA polymerase gene, a thioesterase gene, and an acyl-CoA-synthetase gene. The cells further have one or more genes functionally deleted. The functionally deleted genes include such genes as an enoyl-CoA hydratase gene, a 3-hydroxyacyl-CoA dehydrogenase, and a 3-ketoacyl-CoA thiolase gene. The recombinant cells are capable of using producing polyhydroxyalkanoates with a high proportion of monomers having the same carbon length from non-lipid substrates, such as carbohydrates.

The invention describes a process for preparing acetone starting from acetyl-coenzyme A comprising process steps A. enzymatic conversion of acetyl-CoA into acetoacetyl-CoA B. enzymatic conversion of acetoacetyl-CoA into acetoacetate and CoA and C. decarboxylation of acetoacetate to acetone and CO2, which is characterized in that the coenzyme A is not transferred in process step B to an acceptor molecule. In addition, process step B is surprisingly catalyzed by enzymes of the classes of acyl-CoA thioesterase, acyl-CoA synthetase or acyl-CoA thiokinase.A completely novel metabolic pathway is concerned, because the enzymatic hydrolysis of acetoacetyl-CoA without simultaneous transfer of CoA to a receptor molecule has never previously been described for any microbial enzyme.

The invention relates to a method for synthesizing biodiesel with microorganisms in vivo, which is realized in escherichia coli. The method comprises the following steps of: respectively cloning an acinetobacter wax fat synthetase gene atfA, an escherichia coli acyl coenzyme A synthetase gene fadD, a zymomonas mobilis pyruvate decarboxylase gene pdc and an alcohol dehydrogenase gene adhB gene on a pET expression vector in series to obtain a plasmid pXT11; transferring the plasmid pXT11 into escherichia coli containing a plasmid pMSD8 and a plasmid pMSD15 to obtain an escherichia coli stain XT31; and generating biodiesel by the escherichia coli stain XT31. The method realizes the microbial transformation from sugar to the biodiesel, lays the foundation for biologically preparing the biodiesel from lignocelluloses, and radically solves the problem of insufficient raw material supply in biodiesel preparation. A step of esterifying methanol is not needed in the technology, thereby the cost is greatly reduced and the problems that glycerol as a side product is formed, and the like are avoided.

The invention discloses a kit and method for clinically detecting serum or plasma free fatty acid. The kit is composed of a reagent 1 and a reagent 2, wherein the reagent 1 comprises a buffer, ATP, a coenzyme A, 4-amino antipyrine, an ion activator, an acyl coenzyme A synthetase, stabilizer, a preservative, a surfactant, and concentrated hydrochloric acid, and the reagent 2 comprises a buffer, a chromogen, a composite sulfhydryl reagent, a peroxidase, an acyl coenzyme A oxidase, a stabilizer, a preservative, a surfactant and concentrated hydrochloric acid. The kit has the advantages of good stability, high specificity of the free fatty acid, and wide linear range. The serum or plasma free fatty acid is detected by the enzyme method, and the method has the advantages of high precision, andsmall measuring error.