(R,R)-butanediol dehydrogenase
In enzymology, a (R,R)-butanediol dehydrogenase (EC 1.1.1.4) is an enzyme that catalyzes the chemical reaction
- (R,R)-butane-2,3-diol + NAD+ (R)-acetoin + NADH + H+
| (R,R)-butanediol dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Meso-2,3-butanediol dehydrogenase from Klebsiella pneumoniae. PDB 1geg | |||||||||
| Identifiers | |||||||||
| EC number | 1.1.1.4 | ||||||||
| CAS number | 37250-09-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are (R,R)-butane-2,3-diol and NAD+, whereas its 3 products are (R)-acetoin, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R,R)-butane-2,3-diol:NAD+ oxidoreductase. Other names in common use include butyleneglycol dehydrogenase, D-butanediol dehydrogenase, D-(−)-butanediol dehydrogenase, butylene glycol dehydrogenase, diacetyl (acetoin) reductase, D-aminopropanol dehydrogenase, D-aminopropanol dehydrogenase, 1-amino-2-propanol dehydrogenase, 2,3-butanediol dehydrogenase, D-1-amino-2-propanol dehydrogenase, (R)-diacetyl reductase, (R)-2,3-butanediol dehydrogenase, D-1-amino-2-propanol:NAD+ oxidoreductase, 1-amino-2-propanol oxidoreductase, and aminopropanol oxidoreductase. This enzyme participates in butanoic acid metabolism.
References
- Strecker HJ, Harary I (November 1954). "Bacterial butylene glycol dehydrogenase and diacetyl reductase". The Journal of Biological Chemistry. 211 (1): 263–70. PMID 13211662.
- Taylor MB, Juni E (April 1960). "Stereoisomeric specificities of 2,3-butanediol dehydrogenases". Biochimica et Biophysica Acta. 39 (3): 448–57. doi:10.1016/0006-3002(60)90197-9. PMID 13837186.