EC Number   |
General Information |
Reference |
|---|
   1.1.1.B20 | 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.B20 | 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.B20 | physiological function |
2,3-butanediol dehydrogenase (BDH) catalyzes the interconversion between acetoin and 2,3-butanediol and is a key enzyme for 2,3-butanediol production |
-, 742149 |
| 1.1.1.B20 | 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.B20 | physiological function |
acetoin can be converted to 2,3-butanediol by 2,3-butanediol dehydrogenase (budC) with consumption of NADH |
-, 761003 |
| 1.1.1.B20 | evolution |
Bdh enzymes can be classified into R-acting or S-acting depending on the chirality of the chiral center introduced by the enzyme at the acetoin C2 atom. Whereas the preference for (3R)-acetoin or (3S)-acetoin is imprinted in the geometry of the substrate-binding pocket, R-acting and S-acting Bdh enzymes belong to different protein families and possess different architectures |
-, 760761 |
| 1.1.1.B20 | physiological function |
budC encodes the major meso-2,3-butanediol dehydrogenase catalyzing the reversible reaction from acetoin to meso-2,3-butanediol in Bacillus licheniformis |
-, 742152 |
| 1.1.1.B20 | physiological function |
D-(-)-acetoin with an optical purity of 25.9% is produced by PT-BDH |
-, 761599 |
| 1.1.1.B20 | physiological function |
D-(-)-acetoin with an optical purity of 57% is produced by BS-BDH |
-, 761599 |
| 1.1.1.B20 | 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 |
