In enzymology, a 3-hydroxybutyryl-CoA epimerase (EC 5.1.2.3) is an enzyme that catalyzes the chemical reaction
| 3-hydroxybutyryl-CoA epimerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.1.2.3 | ||||||||
| CAS no. | 9024-21-9 | ||||||||
| 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 | ||||||||
| |||||||||
- (S)-3-hydroxybutanoyl-CoA (R)-3-hydroxybutanoyl-CoA
Hence, this enzyme has one substrate, (S)-3-hydroxybutanoyl-CoA, and one product, (R)-3-hydroxybutanoyl-CoA.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on hydroxy acids and derivatives. The systematic name of this enzyme class is 3-hydroxybutanoyl-CoA 3-epimerase. Other names in common use include 3-hydroxybutyryl coenzyme A epimerase, and 3-hydroxyacyl-CoA epimerase. This enzyme participates in fatty acid metabolism and butanoate metabolism.
Structural studies
editAs of late 2007, four structures have been solved for this class of enzymes, with PDB accession codes 1WDK, 1WDL, 1WDM, and 2D3T.
References
edit- Stern JR, del Campillo A, Lehninger AL (1955). "Enzymatic racemization of beta-hydroxybutyryl-S-CoA and the stereospecificity of enzymes of the fatty acid cycle". J. Am. Chem. Soc. 77 (4): 1073–1074. doi:10.1021/ja01609a105.
- Wakil SJ (1955). "D(−)beta-Hydroxybutyryl CoA dehydrogenase". Biochim. Biophys. Acta. 18 (2): 314–315. doi:10.1016/0006-3002(55)90089-5. PMID 13276396.
