EC Number   |
General Information |
Reference  |
|---|
    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 | 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 |
| 1.1.1.4 | evolution |
the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis |
721872 |
| 1.1.1.4 | evolution |
the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal |
-, 740827 |
| 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 | malfunction |
the amount of (2R,3R)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin |
-, 756608 |
| 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 | metabolism |
the proposed pathway from glucose to 2,3-butanediol in Paenibacillus brasilensis involves the enzyme, overview |
-, 760411 |
| 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 |
two (2R,3R)-2,3-butanediol dehydrogenases (BDHs) from industrial (denoted Y)/laboratory (denoted B) strains of Saccharomyces cerevisiae, Bdh1p(Y)/Bdh1p(B) and Bdh2p(Y)/Bdh2p(B), are members of the PDH subfamily with an NAD(P)H binding domain and a catalytic zinc binding domain, and exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural |
-, 760423 |
