Enzyme

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     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:1.13.11.48
Description:3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase.
Alternative Name: (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase.
Cath: 1.10.210.20; 3.40.50.1820;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.13.11.48
BRENDA Enzyme Link: BRENDA 1.13.11.48
KEGG Enzyme Link: KEGG1.13.11.48
BioCyc Enzyme Link: BioCyc 1.13.11.48
ExPASy Enzyme Link: ExPASy1.13.11.48
EC2PDB Enzyme Link: EC2PDB 1.13.11.48
ExplorEnz Enzyme Link: ExplorEnz 1.13.11.48
PRIAM enzyme-specific profiles Link: PRIAM 1.13.11.48
IntEnz Enzyme Link: IntEnz 1.13.11.48
MEDLINE Enzyme Link: MEDLINE 1.13.11.48
MSA:

1.13.11.48;

Phylogenetic Tree:

1.13.11.48;

Uniprot:
M-CSA:
RHEA:21572 3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = CO + H(+) + N-acetylanthranilate
RULE(radius=1) [*:1]:[c;H0;+0:2]1:[*:3]:[nH;+0:4]:[c;H0;+0:5](-[*:6]):[c;H0;+0:7](-[*:8]):[c;H0;+0:9]:1=[O;H0;+0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:1]:[c;H0;+0:2](:[*:3]-[NH;+0:4]-[C;H0;+0:5](-[*:6])=[O;H0;+0:12])-[C;H0;+0:7](-[*:8])=[O;H0;+0:11].[C-;H0:9]#[O+;H0:10]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
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 F1996 Sep 158856057
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 S2010 Jan 1220080731
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 S1999 Sep10482514
Dioxygenases without requirement for cofactors: identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase.Frerichs-Deeken U, Fetzner S2005 Nov16187153
Dioxygenases without requirement for cofactors and their chemical model reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion.Frerichs-Deeken U, Ranguelova K, Kappl R, Hüttermann J, Fetzner S2004 Nov 1615533053
Molecular cloning, sequencing, expression, and site-directed mutagenesis of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene from Arthrobacter spec. Rü61a.Betz A, Facey SJ, Hauer B, Tshisuaka B, Lingens F200010746195