This disclosure provides a genetically-modified bacterium from the genus Megasphaera that comprises an exogenous nucleic acid encoding a bifunctional aldehyde/alcohol dehydrogenase that produces butanol as the final product. The disclosure further provides methods for producing butanol using such genetically-modified bacterium.

A composition includes two exogenous enzymes from animals for consumption by human beings to prevent, treat and/or alleviate veisalgia and/or symptoms associated therewith arising from or caused by consumption or spontaneous production of alcohol through a dual-enzyme based breakdown of the alcohol, wherein a first enzyme of the two exogenous enzymes is capable of converting alcohol into a first metabolite while a second enzyme thereof is capable of converting the first metabolite into a second metabolite which is excretable to systemic circulation after an oxidation reaction of the alcohol in the presence of the two exogenous enzymes and NAD.sup.+/NADH, and wherein the first enzyme to the second enzyme is in a molar ratio of 1:3-51 in the composition in order to avoid an elevation in the level of the first metabolite in the human being.

The invention provides a non-naturally occurring microbial biocatalyst including a microbial organism having a 4-hydroxybutanoic acid (4-HB) biosynthetic pathway having at least one exogenous nucleic acid encoding 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase, or α-ketoglutarate decarboxylase, wherein the exogenous nucleic acid is expressed in sufficient amounts to produce monomeric 4-hydroxybutanoic acid (4-HB). Also provided is a non-naturally occurring microbial biocatalyst including a microbial organism having 4-hydroxybutanoic acid (4-HB) and 1,4-butanediol (BDO) biosynthetic pathways, the pathways include at least one exogenous nucleic acid encoding 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase, 4-hydroxybutyrate:CoA transferase, 4-butyrate kinase, phosphotransbutyrylase, α-ketoglutarate decarboxylase, aldehyde dehydrogenase, alcohol dehydrogenase or an aldehyde/alcohol dehydrogenase, wherein the exogenous nucleic acid is expressed in sufficient amounts to produce 1,4-butanediol (BDO). Additionally provided are methods for the production of 4-HB and BDO.

The present invention relates to the production of compounds comprised in pheromones, in particular moth pheromones, such as desaturated fatty alcohols and desaturated fatty acyl acetates and derivatives thereof, from a yeast cell.

A yeast strain producing glutathione (GSH) and aldehyde dehydrogenase, and more specifically, the yeast strains Saccharomyces cerevisiae Kwon P-1 KCTC13925BP, Saccharomyces cerevisiae Kwon P-2 KCTC14122BP, and Saccharomyces cerevisiae Kwon P-3 KCTC14123BP, which produce both glutathione and aldehyde dehydrogenase.

Maple syrup urine disease (MSUD) is a rare autosomal recessive disease with an incidence that is caused by a defective activity of the branched-chain 2-keto acid dehydrogenase (BCKD) leading to accumulation of branched-chain amino acids (BCAA) leucine, isoleucine, valine and their corresponding alpha-ketoacids (BCKA) in tissues and body fluids. The inventors herein characterized the Bckdha.sup.−/− mouse and Bckdhb.sup.−/− mouse recapitulating the classical forms of MSUD. As a proof of concept, they developed a (liver-directed) AAV gene therapy based on the transfer of human BCKDHA (hBCKDHA) or BCKDHB (hBCKDHB) mediated by AAV8 during immediate neonatal period in Bckdha−/− or Bckdhb.sup.−/− mice. The inventors demonstrated that hBCKDHA gene transfer completely rescued the lethal early-onset phenotype of Bckdha−/− mice allowing long-term survival to age 12 months, at which they were systematically sacrificed, without overt phenotypic abnormalities. They also demonstrated that hBCKDHB gene transfer exhibited similar survival and a normal growth without overt phenotypic abnormalities at age 3 months, with a dramatic improvement of the biochemical phenotype. The present invention relates to a method of treating MSUD by gene therapy.

Described herein are engineered metabolic pathways in recombinant microorganism host cells which result in the production of 2-phenylethanol or 2-phenylacetic acid. Also described herein are methods of using the recombinant microorganisms for the production of 2-phenylethanol or 2-phenylacetic acid.

The present disclosure provides an engineered microorganism capable of producing malonic acid, malonate, esters of malonic acid, or mixtures thereof. The engineered microorganism includes a malonate-semialdehyde dehydrogenase that is heterologous to a native form of the engineered microorganism and comprises at least 90% sequence identity to any one of SEQ ID Nos: 7, 9, 11, 13, 15, 17, 19, 21, 23, 27, 29, and 31, wherein the engineered microorganism is capable of producing about 9 g/L to about 250 g/L of malonic acid, malonate, esters of malonic acid, or mixtures thereof.

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.

The present invention relates to the field of fungal biotechnology, more particularly to genetic engineering methods for the production of carotenoids in fungal hosts selected from Rhodospordium and Rhodotorula genera.