Enzymes
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- Name help_outline quinolin-8-ol Identifier CHEBI:48981 (CAS: 148-24-3) help_outline Charge 0 Formula C9H7NO InChIKeyhelp_outline MCJGNVYPOGVAJF-UHFFFAOYSA-N SMILEShelp_outline Oc1cccc2cccnc12 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline A Identifier CHEBI:13193 Charge Formula R SMILEShelp_outline * 2D coordinates Mol file for the small molecule Search links Involved in 3,077 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 8-hydroxyquinolin-2(1H)-one Identifier CHEBI:48988 (Beilstein: 472106) help_outline Charge 0 Formula C9H7NO2 InChIKeyhelp_outline ZXZKYYHTWHJHFT-UHFFFAOYSA-N SMILEShelp_outline Oc1cccc2ccc(=O)[nH]c12 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline AH2 Identifier CHEBI:17499 Charge 0 Formula RH2 SMILEShelp_outline *([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 3,005 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:25924 | RHEA:25925 | RHEA:25926 | RHEA:25927 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Microbial metabolism of quinoline and related compounds. VII. Quinoline oxidoreductase from Pseudomonas putida: a molybdenum-containing enzyme.
Bauder R., Tshisuaka B., Lingens F.
The quinoline oxidoreductase from Pseudomonas putida was purified 50-fold to homogeneity with 21% recovery, using ammonium sulfate precipitation, hydrophobic interaction-, anion exchange-, and gel chromatography. The Mr of the native enzyme was calculated to be 300,000 by gel filtration. SDS-polya ... >> More
The quinoline oxidoreductase from Pseudomonas putida was purified 50-fold to homogeneity with 21% recovery, using ammonium sulfate precipitation, hydrophobic interaction-, anion exchange-, and gel chromatography. The Mr of the native enzyme was calculated to be 300,000 by gel filtration. SDS-polyacrylamide gel electrophoresis of the enzyme revealed three protein bands corresponding to Mr 85,000, 30,000 and 20,000. The enzyme contained 8 atoms of iron, 8 atoms of acid-labile sulfide, 2 molecules of FAD, and the molybdenum cofactor, molybdopterin. Besides quinoline, the quinoline oxidoreductase also catalysed the conversion of 5-, 6-, 7- and 8-hydroxyquinoline and 8-chloroquinoline to the corresponding 2-oxo compounds. The incorporated oxygen atom was derived from water. Cyanide and methanol were effective inhibitors. << Less
Biol Chem Hoppe Seyler 371:1137-1144(1990) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.