| Entry |
|
|---|
| Name |
quinoline 2-oxidoreductase |
|---|
| Class |
Oxidoreductases;
Acting on the CH-CH group of donors;
With other acceptors
 |
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| Sysname |
quinoline:acceptor 2-oxidoreductase (hydroxylating) |
|---|
| Reaction(IUBMB) |
quinoline + acceptor + H2O = quinolin-2(1H)-one + reduced acceptor
[RN:R05152] |
|---|
| Reaction(KEGG) |
R05152
 |
|---|
| Substrate |
quinoline [CPD:C06413];
acceptor [CPD:C00028];
H2O [CPD:C00001] |
|---|
| Product |
quinolin-2(1H)-one [CPD:C06415];
reduced acceptor [CPD:C00030] |
|---|
| Comment |
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. |
|---|
| Structures |
PDB: 1T3Q |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:2090161]
Bauder R, Tshisuaka B, 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) 1137-44.
Pseudomonas putida |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:8251516]
Tshisuaka B, Kappl R, Huttermann J, Lingens F.
Quinoline oxidoreductase from Pseudomonas putida 86: an improved
purification procedure and electron paramagnetic resonance
spectroscopy.
Biochemistry. 32 (1993) 12928-34.
Pseudomonas putida |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:1789933]
Peschke B, Lingens F.
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 (1991) 1081-8.
Pseudomonas putida, Rhodococcus sp. |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:7556204]
Schach S, Tshisuaka B, Fetzner S, 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) 536-44.
Comamonas testosteroni |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.3.99.17
IUBMB Enzyme Nomenclature: 1.3.99.17
ExPASy - ENZYME nomenclature database: 1.3.99.17
UM-BBD (Biocatalysis/Biodegradation Database): 1.3.99.17
BRENDA, the Enzyme Database: 1.3.99.17
CAS: 132264-32-5 |
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