EC Number   |
General Information |
Reference |
|---|
    1.1.1.4 | physiological function |
22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon |
-, 756608 |
| 1.1.1.4 | physiological function |
acetoin and 2,3-butanediol can be transformed into each other by 2,3-butanediol dehydrogenase (BDH) using NADH/NAD+ as coenzyme. The main 2,3-butanediol production of strain BS168D is meso-2,3-butanediol and the bdhA gene is only responsible for (2R,3R)-2,3-butanediol synthesis. Oxygen supply in the culture of Bacillus subtilis has an important impact on the product yield, productivity and 2,3-butanediol formation in acetoin fermentation. In general, high oxygen supply favours acetoin formation and decrease 2,3-butanediol final yield |
-, 762259 |
| 1.1.1.4 | metabolism |
BDH2 is a gene adjacent to BDH1, and these genes are regulated reciprocally. BDH2 is only responsible for converting diacetyl into acetoin, but not for the metabolic pathway of acetoin to 2,3-butanediol in Saccharomyces uvarum |
-, 761646 |
| 1.1.1.4 | physiological function |
deletion of BDH1 results in an accumulation of acetoin and a diminution of 2,3-butanediol in two Saccharomyces cerevisiae strains under two different growth conditions |
710944 |
| 1.1.1.4 | malfunction |
deletion of bdhA gene successfully blocks the reversible transformation between acetoin and 2,3-butanediol and eliminates the effect of dissolved oxygen on the transformation |
-, 762259 |
| 1.1.1.4 | evolution |
enzyme BtBDH contains a GroES-like domain at the N terminus and a NAD(P)-binding domain at the C-terminus. Phylogenetic tree analysis reveals that BtBDH is a member ofthe (2R,3R)-2,3-BDH group. BtBDH has the typical (2R,3R)-2,3-butanediol dehydrogenase properties and belongs to the MDR superfamily. According to previous reports, (2R,3R)-2,3-BDH generally belongs to the MDR family, while meso-2,3-BDH is commonly clustered in the SDR (short chain dehydrogenase/reductase) family |
-, 760463 |
| 1.1.1.4 | physiological function |
glycerol/1,2-propanediol dehydrogenase GldA is the major enzyme responsible for the acetoin reducing activity observed in Escherichia coli |
-, 740952 |
| 1.1.1.4 | metabolism |
overview of 2,3-BDL biosynthesis pathway and byproducts in microaerobic conditions of Paenibacillus polymyxa strain DSM 365 starting from sucrose as a substrate |
-, 761810 |
| 1.1.1.4 | physiological function |
Paenibacillus brasilensis produces 2,3-butanediol (2,3-BDO). And although the gene encoding (S,S)-2,3-butanediol dehydrogenase (EC 1.1.1.76) is found in the genome of Paenibacillus brasilensis strain PB24, only R,R-2,3-butanediol ((R,R)-2,3-butanediol dehydrogenase, EC 1.1.1.4) and meso-2,3-butanediol are detected by gas chromatography under the growth conditions tested. The enzyme is multifunctional as R,R-2,3-butanediol dehydrogenase/meso-2,3-butanediol dehydrogenase/diacetyl reductase |
-, 760411 |
| 1.1.1.4 | evolution |
the (2R,3R)-2,3-butanediol dehydrogenase belongs to the mostly zinc-containing medium-chain dehydrogenase/reductase superfamily and not to the short-chain dehydrogenase/reductase superfamily, to which meso- and (2S,3S)-2,3-butanediol dehydrogenases belong, phylogenetic analysis. The enzyme contains two hydrophobic residues forming the binding site for cofactor NAD(P), Phe138 and Leu141 (numbers refer to R,R-BDH of Saccharomyces cerevisiae) |
-, 721345 |
