Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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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: ?


Enzymatic reaction of: quinoline 2-oxidoreductase

3-methylquinoline + an oxidized electron acceptor + H2O <=> 3-methyl-2-oxo-1,2-dihydroquinoline + a reduced electron acceptor

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

Summary:
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)

Summary:
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)


References

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, BIOCYC14B.