In enzymology, an isoquinoline 1-oxidoreductase (EC 1.3.99.16) is an enzyme that catalyzes the chemical reaction
| 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 | ||||||||
| |||||||||
- isoquinoline + acceptor + H2O isoquinolin-1(2H)-one + reduced acceptor
The 3 substrates of this enzyme are isoquinoline, acceptor, and H2O, whereas its two products are isoquinolin-1(2H)-one and reduced acceptor.
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
edit- 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. 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.
