Methods and systems for producing prescribed unit size poly(3-hydroxyalkanoate) (PHA) polymers and copolymers are provided. The methods and systems can employ recombinant bacteria that are not native producers of PHA or lack enzymes to degrade PHA once synthesized, metabolize short to long chain fatty acids without induction, and express an (R)-specific enoyl-CoA hydratase and a PHA synthase, the (R)-specific enoyl-CoA hydratase and PHA synthase having wide substrate specificities. The recombinant bacteria are fed at least one fatty acid substrate that is equal in carbon length to the prescribed or desired unit size of the PHA polymer to be produced. The prescribed unit size PHA that is produced is then isolated and/or purified.

This document relates to using bidirectional, multi-enzymatic scaffolds to biosynthesize cannabinoids in recombinant hosts.

The invention provides a non-naturally occurring microbial organism having a microbial organism having at least one exogenous gene insertion and/or one or more gene disruptions that confer production of primary alcohols. A method for producing long chain alcohols includes culturing these non-naturally occurring microbial organisms.

The invention provides non-naturally occurring microbial organisms containing a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms selectively produce a fatty alcohol, fatty aldehyde or fatty acid of a specified length. Also provided are non-naturally occurring microbial organisms having a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms further include an acetyl-CoA pathway. In some aspects, the microbial organisms of the invention have select gene disruptions or enzyme attenuations that increase production of fatty alcohols, fatty aldehydes or fatty acids. The invention additionally provides methods of using the above microbial organisms to produce a fatty alcohol, a fatty aldehyde or a fatty acid.

The present invention relates to the metabolic engineering of a microbial host for the synthesis of value-added products from oil palm empty fruit brunches (OPEFBs). In one embodiment, the genetically engineered microorganism is Escherichia coli comprising a metabolic pathway consisting of 9 enzymes (11 genes) to utilize depolymerized lignin, namely vanillin, p-coumaric acid, p-hydroxybenzaldehyde, vanillic acid, p-hydroxybenzoic acid and ferulic acid, to produce β-ketoadipic acid, which can be subsequently converted into commercially important derivatives such as adipic acid and levulinic acid. The enzymes are feruloyl-CoA synthetase (fcs), enoyl-CoA hydratase (ech), vanillin dehydrogenase (vdh), vanillate O-demethylase (vanA; vanA and vanB), p-hydroxy benzoate hydroxylase (pobA), protocatechuate 3,4-dioxygenase {pcaGH; pcaG and pcaH), 3-carboxy-cis, cis-muconate cycloisomerase (pcaB), 4-carboxymuconolactone decarboxylase (pcaC), and β-ketoadipate enol-lactone hydrolase (pcaD).

Described is a method for the production of 3-buten-2-one comprising the enzymatic conversion of 4-hydroxy-2-butanone into 3-buten-2-one by making use of an enzyme catalyzing 4-hydroxy-2-butanone dehydration, wherein said enzyme catalyzing 4-hydroxy-2-butanone dehydration is (a) a 3-hydroxypropiony-CoA dehydratase (EC 4.2.1.116), (b) a 3-hydroxybutyryl-CoA dehydratase (EC 4.2.1.55), (c) an enoyl-CoA hydratase (EC 4.2.1.17), (d) a 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59), (e) a crotonyl-[acyl-carrier-protein] hydratase (EC 4.2.1.58), (f) a 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.60), (g) a 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.61), (h) a long-chain-enoyl-CoA hydratase (EC 4.2.1.74), or (i) a 3-methylglutaconyl-CoA hydratase (EC 4.2.1.18). The produced 3-buten-2-one can be further converted into 3-buten-2-ol and finally into 1,3-butadiene.

Recombinant cells and methods for producing methyl ketones, such as medium-chain methyl ketones. The recombinant cells include recombinant acyl-ACP thioesterase genes, recombinant β-ketoacyl-CoA thioesterase genes, and recombinant acyl-CoA synthetase genes, in addition to other modifications. The methods include culturing the recombinant cells to produce the methyl ketones and isolating the produced methyl ketones.

A recombinant host cell capable of biosynthesizing cannabichromenic acid and a construction method thereof, and a method for biosynthesizing cannabichromenic acid through the recombinant host cell. Saccharomyces cerevisiae is taken as a host. First, cannabigerolic acid synthase and cannabichromenic acid synthase are over-expressed in the host; then, a metabolic pathway of a precursor compound, olivetolic acid, synthesizing cannabichromenic acid from saccharides is constructed in the host, a metabolic pathway for hexanoic acid to olivetolic acid is further constructed in the host, an endogenous mevalonate pathway of the host and a metabolic pathway of acetyl-CoA are optimized, cannabichromenic acid synthase is rationally designed, highly active cannabichromenic acid synthase is screened out, and finally, a cannabichromene pathway is located to peroxisomes and lipid droplets by using the cell compartmentalization principle to obtain recombinant Saccharomyces cerevisiae capable of biosynthesizing cannabichromenic acid.

An object of the present invention is to provide enzymes and a DNA encoding the enzymes that are involved in biosynthesis of trehangelin which has the potential to be a therapeutic agent for photosensitivity disorder and cosmetics, and to provide a method for producing trehangelin by utilizing the enzymes and a recombinant microorganism. The present invention is directed to a protein having an amino acid sequence of SEQ ID NO: 3, 5, 7 or 9, or a protein having an amino acid sequence of SEQ ID NO: 3, 5, 7 or 9 in which one to several amino acids are deleted, substituted, added and/or inserted or an amino acid sequence having 60% or more homology with the amino acid sequence of SEQ ID NO: 3, 5, 7 or 9 and having an enzyme activity involved in biosynthesis of trehangelin; and a DNA encoding said protein.

Described is a method for the conversion of 3-methylcrotonyl-CoA into 3-hydroxy-3-methylbutyric acid comprising the steps of:

(a) enzymatically converting 3-methylcrotonyl-CoA into 3-hydroxy-3-methylbutyryl-CoA; and
(b) further enzymatically converting the thus produced 3-hydroxy-3-methylbutyryl-CoA into 3-hydroxy-3-methylbutyric acid
wherein the enzymatic conversion of 3-hydroxy-3-methylbutyryl-CoA into 3-hydroxy-3-methylbutyric acid according to step (b) is achieved by first converting 3-hydroxy-3-methylbutyryl-CoA into 3-hydroxy-3-methylbutyryl phosphate and then subsequently converting the thus produced 3-hydroxy-3-methylbutyryl phosphate into 3-hydroxy-3-methylbutyric acid.