EC Number   |
General Information |
Reference |
|---|
    1.1.1.76 | evolution |
the enzyme belongs to the family of the short-chain dehydrogenase/reductases |
-, 721396 |
| 1.1.1.76 | evolution |
the enzyme belongs to the short-chain dehydrogenases/reductases |
761081 |
| 1.1.1.76 | malfunction |
the amount of (2S,3S)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The disruption of locus pa4148, encoding (2S,3S)-2,3-BDH, partially impairs the growth of this strain in (2S,3S)-2,3-BD but does not affect its growth in (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4148 mutant strain with its gene successfully restores the growth ability. The DELTApa4148 PAO1 strain can grow in racemic acetoin, indicating that (2S,3S)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin |
-, 756608 |
| 1.1.1.76 | metabolism |
2,3-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 |
| 1.1.1.76 | metabolism |
the proposed pathway from glucose to 2,3-butanediol in Paenibacillus brasilensis involves the enzyme, overview |
-, 760411 |
| 1.1.1.76 | more |
identification of the the active tunnel of meso-2,3-BDH. The two short alpha-helices positioned away from the alpha4-helix possibly expose the hydrophobic ligand-binding cavity, gating the exit of product and cofactor from the activity pocket. AC binds in the active pocket including Ser139, Gln140, Ala141, Leu149, Tyr152, Gly183, Ile184, and Trp190. Residues Phe212 and Asn146 function as the key product-release sites. Three catalytic residues are Ser139, Tyr152, and Lys156. Docking study using the structure of meso-2,3-BDH (PDB ID 1GEG), molecular dynamics simulation |
761081 |
| 1.1.1.76 | physiological function |
2,3-butanediol (2,3-BD) is a primary microbial metabolite that enhances the virulence of Pseudomonas aeruginosa and alters the lung microbiome. 2,3-BD exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD |
-, 756608 |
| 1.1.1.76 | physiological function |
besides encoding diacetyl reductase, the butA gene is also responsible for the expression of S-2,3-butanediol dehydrogenase, which may direct the pathway for production of S,S-2,3-BDO and meso-2,3-BDO |
-, 760411 |
| 1.1.1.76 | 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 |
| 1.1.1.76 | physiological function |
the meso-2,3-butanediol dehydrogenase (meso-2,3-BDH) catalyzes NAD+-dependent conversion of meso-2,3-butanediol to acetoin (AC), a crucial external energy storage molecule in fermentive bacteria. The interconversion between (3R)-AC and meso-2,3-BD or (3S)-AC and (2S,3S)-2,3-BD is catalyzed by meso-2,3-butanediol dehydrogenase (meso-2,3-BDH) |
761081 |
