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
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 (12): 1137–44.
doi:
10.1515/bchm3.1990.371.2.1137.
PMID2090161.
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 (47): 12928–34.
doi:
10.1021/bi00210a047.
PMID8251516.
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 (12): 1081–8.
doi:
10.1515/bchm3.1991.372.2.1081.
PMID1789933.
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 (2): 536–44.
doi:
10.1111/j.1432-1033.1995.tb20841.x.
PMID7556204.