EC Number   |
General Information |
Reference |
|---|
    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 | 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 R-selective 2,3-butanediol dehydrogenase from Bacillus clausii strain DSM 8716 (BcBDH) belongs to the metal-dependent medium chain dehydrogenases/reductases family (MDR) |
-, 762382 |
| 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 | 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 |
| 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 | 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 | 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 | 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 |
