In enzymology, a 3alpha-hydroxyglycyrrhetinate dehydrogenase (EC 1.1.1.230) is an enzyme that catalyzes the chemical reaction
| 3-alpha-hydroxyglycyrrhetinate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.230 | ||||||||
| CAS no. | 114308-07-5 | ||||||||
| 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 | ||||||||
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- 3alpha-hydroxyglycyrrhetinate + NADP+ 3-oxoglycyrrhetinate + NADPH + H+
Thus, the two substrates of this enzyme are 3alpha-hydroxyglycyrrhetinate and NADP+, whereas its 3 products are 3-oxoglycyrrhetinate, NADPH, 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-hydroxyglycyrrhetinate:NADP+ 3-oxidoreductase.
References
edit- Akao T, Akao T, Hattori M, Namba T, Kobashi K (March 1988). "Purification and properties of 3 alpha-hydroxyglycyrrhetinate dehydrogenase of Clostridium innocuum from human intestine". J. Biochem. 103 (3): 504–7. PMID 3164718.
