| EC |
1.3.99.17 |
| Accepted name: |
quinoline 2-oxidoreductase |
| Reaction: |
quinoline + acceptor + H2O = quinolin-2(1H)-one + reduced acceptor |
| Systematic name: |
quinoline:acceptor 2-oxidoreductase (hydroxylating) |
| Comments: |
Quinolin-2-ol, quinolin-7-ol, quinolin-8-ol, 3-, 4- and 8-methylquinolines and 8-chloroquinoline are substrates. Iodonitrotetrazolium chloride can act as an electron acceptor. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 132264-32-5 |
| References: |
| 1. |
Bauder, R., Tshisuaka, B. and Lingens, F. Microbial metabolism of quinoline and related compounds. VII. Quinoline oxidoreductase from Pseudomonas putida: a molybdenum-containing enzyme. Biol. Chem. Hoppe-Seyler 371 (1990) 1137–1144. [PMID: 2090161] |
| 2. |
Tshisuaka, B., Kappl, R., Huttermann, J. and Lingens, F. Quinoline oxidoreductase from Pseudomonas putida 86: an improved purification procedure and electron paramagnetic resonance spectroscopy. Biochemistry 32 (1993) 12928–12934. [PMID: 8251516] |
| 3. |
Peschke, B. and Lingens, F. Microbial metabolism of quinoline and related compounds. XII. Isolation and characterization of the quinoline oxidoreductase from Rhodococcus sp. B1 compared with the quinoline oxidoreductase from Pseudomonas putida 86. Biol. Chem. Hoppe-Seyler 372 (1991) 1081–1088. [PMID: 1789933] |
| 4. |
Schach, S., Tshisuaka, B., Fetzner, S. and Lingens, F. 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 (1995) 536–544. [DOI] [PMID: 7556204] |
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| [EC 1.3.99.17 created 1999] |
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