3alpha-hydroxycholanate dehydrogenase

In enzymology, a 3alpha-hydroxycholanate dehydrogenase (EC 1.1.1.52) is an enzyme that catalyzes the chemical reaction

3-alpha-hydroxycholanate dehydrogenase
Identifiers
EC no.1.1.1.52
CAS no.9028-57-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
 
 
 
H+
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
H+
 
 

The two substrates of this enzyme are the bile acid lithocholic acid and nicotinamide adenine dinucleotide (NAD+). Its products are dehydrolithocholic acid, NADH, and a proton.[1][2]

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

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As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1IHI.

References

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  1. Enzyme 1.1.1.52 at KEGG Pathway Database.
  2. 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.