| quinoline 2-oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.99.17 | ||||||||
| CAS no. | 132264-32-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a quinoline 2-oxidoreductase ( EC 1.3.99.17) is an enzyme that catalyzes the chemical reaction
- quinoline + acceptor + H2O quinolin-1(2H)-one + reduced acceptor
The 3 substrates of this enzyme are quinoline, acceptor, and H2O, whereas its two products are quinolin-1(2H)-one and reduced acceptor.
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. PMID 2090161.
- 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. PMID 8251516.
- 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. PMID 1789933.
- 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. PMID 7556204.
| quinoline 2-oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.99.17 | ||||||||
| CAS no. | 132264-32-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a quinoline 2-oxidoreductase ( EC 1.3.99.17) is an enzyme that catalyzes the chemical reaction
- quinoline + acceptor + H2O quinolin-1(2H)-one + reduced acceptor
The 3 substrates of this enzyme are quinoline, acceptor, and H2O, whereas its two products are quinolin-1(2H)-one and reduced acceptor.
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. PMID 2090161.
- 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. PMID 8251516.
- 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. PMID 1789933.
- 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. PMID 7556204.