| 3-alpha-hydroxycholanate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.52 | ||||||||
| CAS no. | 9028-57-3 | ||||||||
| 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 3alpha-hydroxycholanate dehydrogenase (EC 1.1.1.52) is an enzyme that catalyzes the chemical reaction
- 3alpha-hydroxy-5beta-cholanate + NAD+ 3-oxo-5beta-cholanate + NADH + H+
Thus, the two substrates of this enzyme are 3alpha-hydroxy-5beta-cholanate and NAD+, whereas its 3 products are 3-oxo-5beta-cholanate, 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 3alpha-hydroxy-5beta-cholanate:NAD+ oxidoreductase. This enzyme is also called alpha-hydroxy-cholanate dehydrogenase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1IHI.
References
- Hayaishi O, Sato Y, Jakoby WB, Stohlman EF (1955). "Reversible enzymatic oxidation of bile acids". Arch. Biochem. 56 (2): 554–5. doi:10.1016/0003-9861(55)90278-2. PMID 14377608.
This page was last edited on 26 August 2023, at 12:38