Isoquinoline 1-oxidoreductase
| isoquinoline 1-oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.99.16 | ||||||||
| CAS no. | 155948-73-5 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, isoquinoline 1-oxidoreductase (EC 1.3.99.16) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are isoquinoline, an electron acceptor, and water. Its products are isocarbostyril and reduced acceptor.[1][2][3]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is isoquinoline:acceptor 1-oxidoreductase (hydroxylating).
References
- ^ Enzyme 1.3.99.16 at KEGG Pathway Database.
- ^ Lehmann M, Tshisuaka B, Fetzner S, Roger P, Lingens F (1994). "Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase". J. Biol. Chem. 269 (15): 11254–60. doi:10.1016/S0021-9258(19)78118-6. PMID 8157655.
- ^ Lehmann M, Tshisuaka B, Fetzner S, Lingens F (1995). "Molecular cloning of the isoquinoline 1-oxidoreductase genes from Pseudomonas diminuta 7, structural analysis of iorA and iorB, and sequence comparisons with other molybdenum-containing hydroxylases". J. Biol. Chem. 270 (24): 14420–9. doi:10.1074/jbc.270.24.14420. PMID 7782304.