MetaCyc Enzyme: quinoline 2-oxidoreductase

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)

Gene-Reaction Schematic

Gene-Reaction Schematic

Enzymatic reaction of: quinoline 2-oxidoreductase

Inferred from experiment

3-methylquinoline + an oxidized unknown electron acceptor + H2O → 3-methyl-2-oxo-1,2-dihydroquinoline + an reduced unknown electron acceptor

The direction shown, i.e. which substrates are on the left and right sides, 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.

Cofactors or Prosthetic Groups: Mo2+ [Schach95], Fe2+ [Schach95], S2- [Schach95], FAD [Schach95]

Subunit of quinoline 2-oxidoreductase: quinoline 2-oxidoreductase α subunit

Molecular Weight: 87 kD (experimental)

Subunit of quinoline 2-oxidoreductase: quinoline 2-oxidoreductase β subunit

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.

Citations: [Schach95]

Subunit of quinoline 2-oxidoreductase: quinoline 2-oxidoreductase γ subunit

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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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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