Quinoline 2-oxidoreductase
| quinoline 2-oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.99.17 | ||||||||
| CAS no. | 132264-32-5 | ||||||||
| 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, quinoline 2-oxidoreductase (EC 1.3.99.17) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are quinoline, an electron acceptor, and water. Its products are 2-quinolone and reduced acceptor.[1][2][3][4]
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 quinoline:acceptor 2-oxidoreductase (hydroxylating).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1T3Q.
References
- ^ Enzyme 1.3.99.17 at KEGG Pathway Database.
- ^ Bauder, Renate; Tshisuaka, Barbara; Lingens, Franz (1990). "Microbial Metabolism of Quinoline and Related Compounds. VII. Quinoline Oxidoreductase from Pseudomonas putida: A Molybdenum-Containing Enzyme". Biological Chemistry Hoppe-Seyler. 371 (2): 1137–1144. doi:10.1515/bchm3.1990.371.2.1137. PMID 2090161.
- ^ Peschke, Bernd; Lingens, Franz (1991). "Microbial Metabolism of Quinoline and Related Compounds. XII. Isolation and Characterization of the Quinoline Oxidoreductase from Rhodococcus spec. B1 Compared with the Quinoline Oxidoreductase from Pseudomonas putida 86". Biological Chemistry Hoppe-Seyler. 372 (2): 1081–1088. doi:10.1515/bchm3.1991.372.2.1081. PMID 1789933.
- ^ Schach, Susanne; Tshisuaka, Barbara; Fetzner, Susanne; Lingens, Franz (1995). "Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63. The First Two Enzymes in Quinoline and 3-methylquinoline Degradation". European Journal of Biochemistry. 232 (2): 536–544. doi:10.1111/j.1432-1033.1995.536zz.x.