Quinoline 2-oxidoreductase

From Wikipedia, the free encyclopedia

In enzymology, a quinoline 2-oxidoreductase (EC 1.3.99.17) is an enzyme that catalyzes the chemical reaction

quinoline + acceptor + H₂O $\rightleftharpoons$ isoquinolin-1(2H)-one + reduced acceptor

The 3 substrates of this enzyme are quinoline, 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 quinoline:acceptor 2-oxidoreductase (hydroxylating).

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1T3Q.

[edit] References

IUBMB entry for 1.3.99.17
BRENDA references for 1.3.99.17 (Recommended.)
PubMed references for 1.3.99.17
PubMed Central references for 1.3.99.17
Google Scholar references for 1.3.99.17
Bauder R, Tshisuaka B, Lingens F (1990). "Microbial metabolism of quinoline and related compounds. VII Quinoline oxidoreductase from Pseudomonas putida: a molybdenum-containing enzyme". Biol. Chem. Hoppe. Seyler. 371: 1137–44. PMID 2090161.
Tshisuaka B, Kappl R, Huttermann J, Lingens F (1993). "Quinoline oxidoreductase from Pseudomonas putida 86: an improved purification procedure and electron paramagnetic resonance spectroscopy". Biochemistry. 32: 12928–34. doi:10.1021/bi00210a047. PMID 8251516.
Peschke B, Lingens F (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". Biol. Chem. Hoppe. Seyler. 372: 1081–8. PMID 1789933.
Schach S, Tshisuaka B, Fetzner S, Lingens F (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". Eur. J. Biochem. 232: 536–44. doi:10.1111/j.1432-1033.1995.tb20841.x. PMID 7556204.