EC Tree |
1. Oxidoreductases |
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases) |
1.13.11 With incorporation of two atoms of oxygen |
ID: | 1.13.11.47 |
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Description: | 3-hydroxy-4-oxoquinoline 2,4-dioxygenase. |
Alternative Name: |
Quinoline-3,4-diol 2,4-dioxygenase. 3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase. 3-hydroxy-4(1H)-one, 2,4-dioxygenase. (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase. |
Cath: | 1.10.210.20; 3.40.50.1820; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 1.13.11.47 |
BRENDA Enzyme Link: | BRENDA 1.13.11.47 |
KEGG Enzyme Link: | KEGG1.13.11.47 |
BioCyc Enzyme Link: | BioCyc 1.13.11.47 |
ExPASy Enzyme Link: | ExPASy1.13.11.47 |
EC2PDB Enzyme Link: | EC2PDB 1.13.11.47 |
ExplorEnz Enzyme Link: | ExplorEnz 1.13.11.47 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.13.11.47 |
IntEnz Enzyme Link: | IntEnz 1.13.11.47 |
MEDLINE Enzyme Link: | MEDLINE 1.13.11.47 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:17949 | 3-hydroxy-1H-quinolin-4-one + O2 = CO + H(+) + N-formylanthranilate |
RULE(radius=1) | [*:1]=[c;H0;+0:2]1:[*:3]:[*:4]:[nH;+0:5]:[cH;+0:6]:[c;H0;+0:7]:1-[OH;+0:8].[O;H0;+0:9]=[O;H0;+0:10]>>[*:1]=[C;H0;+0:2](-[OH;+0:10])-[*:3]:[*:4]-[NH;+0:5]-[CH;+0:6]=[O;H0;+0:9].[C-;H0:7]#[O+;H0:8] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
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2,4-dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Rü61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1. | Bauer I, Max N, Fetzner S, Lingens F | 1996 Sep 15 | 8856057 |
Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold. | Steiner RA, Janssen HJ, Roversi P, Oakley AJ, Fetzner S | 2010 Jan 12 | 20080731 |
Microbial metabolism of quinoline and related compounds. XIV. Purification and properties of 1H-3-hydroxy-4-oxoquinoline oxygenase, a new extradiol cleavage enzyme from Pseudomonas putida strain 33/1. | Block DW, Lingens F | 1992 Jun | 1515060 |
Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases. | Fischer F, Künne S, Fetzner S | 1999 Sep | 10482514 |
Cloning, sequence analysis, and expression of the Pseudomonas putida 33/1 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase gene, encoding a carbon monoxide forming dioxygenase. | Max N, Betz A, Facey S, Lingens F, Hauer B, Fetzner S | 1999 May 18 | 10350631 |