Species: Comamonas testosteroni 63
Subunit composition of quinoline 2-oxidoreductase = [quinoline 2-oxidoreductase α subunit]2[quinoline 2-oxidoreductase β subunit]2[quinoline 2-oxidoreductase γ subunit]2
Molecular Weight: 360 kD (experimental)
Enzymatic reaction of: quinoline 2-oxidoreductase
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
In Pathways: 3-methylquinoline degradation
This enzyme catalyzes the first hydroxylation step in the degradation of 3-methylquinoline. It belongs to the molybdo-iron/sulfur flavoproteins, and contains FAD, molybdenum, iron, and acid-labile sulfur in the stoichiometric ratio of 2:2:8:8. The N-terminal amino acid sequences show high homology to several prokaryotic molybdenum-containing hydroxylases.
Molecular Weight: 87 kD (experimental)
Molecular Weight: 32 kD (experimental)
N-terminal amino acid sequences show strong similarities to quinoline 2-oxidoreductases from Pseudomonas putida 63, and Rhodococcus sp. B1, and to quinoline-4-carboxylic acid 2-oxidoreductase from Agrobacterium sp. 1B.
Molecular Weight: 22 kD (experimental)
Schach95: 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 1995;232(2);536-44. PMID: 7556204
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