5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase
| 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
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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In
enzymology, a 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase (EC 1.3.1.65) is an enzyme that catalyzes the chemical reaction
- 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline + NAD+ 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline + NADH + H+
Thus, the two
substrates of this enzyme are 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline and NAD+, whereas its 3 products are 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline, NADH, and H+
.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline:NAD+ oxidoreductase.
References
- Schach S, Schwarz G, Fetzner S, Lingens F (1993). "Microbial metabolism of quinoline and related compounds. XVII Degradation of 3-methylquinoline by Comamonas testosteroni 63". Biol. Chem. Hoppe-Seyler. 374 (3): 175–81. PMID 8489738.
