3-hydroxy-2-methylbutyryl-CoA dehydrogenase
| 3-hydroxy-2-methylbutyryl-CoA dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.178 | ||||||||
| CAS no. | 52227-66-4 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a 3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC 1.1.1.178) is an enzyme that catalyzes the chemical reaction
- (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ 2-methylacetoacetyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA and NAD+, whereas its 3 products are 2-methylacetoacetyl-CoA, 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 (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA:NAD+ oxidoreductase. Other names in common use include 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase, 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase, and 2-methyl-3-hydroxy-butyryl CoA dehydrogenase. This enzyme participates in valine, leucine and isoleucine degradation.
Structural studies
[edit]As of 20 January 2010, 6 structure have been solved for this class of enzymes, with the PDB accession code 1E3S, 1E3W, 1E6W, 1SO8, 1U7T, 2O23.
References
[edit]- Conrad RS, Massey LK, Sokatch JR (1974). "D- and L-isoleucine metabolism and regulation of their pathways in Pseudomonas putida". J. Bacteriol. 118 (1): 103–11. doi:10.1128/JB.118.1.103-111.1974. PMC 246645. PMID 4150713.
