EC number:1.13.11.8

Enzyme

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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:1.13.11.8
Description:Protocatechuate 4,5-dioxygenase.
Alternative Name: Protocatechuate 4,5-oxygenase.
Cath: 1.10.700.10; 3.40.830.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.13.11.8
BRENDA Enzyme Link: BRENDA 1.13.11.8
KEGG Enzyme Link: KEGG1.13.11.8
BioCyc Enzyme Link: BioCyc 1.13.11.8
ExPASy Enzyme Link: ExPASy1.13.11.8
EC2PDB Enzyme Link: EC2PDB 1.13.11.8
ExplorEnz Enzyme Link: ExplorEnz 1.13.11.8
PRIAM enzyme-specific profiles Link: PRIAM 1.13.11.8
IntEnz Enzyme Link: IntEnz 1.13.11.8
MEDLINE Enzyme Link: MEDLINE 1.13.11.8

EC number:1.13.11.8

MSA:

1.13.11.8;
Phylogenetic Tree:

1.13.11.8;
Uniprot:
M-CSA:
RHEA:24044 3,4-dihydroxybenzoate + O2 = 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+)
RULE(radius=1) [*:1]-[c;H0;+0:2]1:[cH;+0:3]:[c;H0;+0:4](-[OH;+0:5]):[c;H0;+0:6](-[OH;+0:7]):[cH;+0:8]:[cH;+0:9]:1.[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[C;H0;+0:2](=[CH;+0:3]-[CH;+0:4]=[O;H0;+0:5])-[CH;+0:9]=[C;H0;+0:8](-[OH;+0:10])-[C;H0;+0:6](=[O;H0;+0:7])-[OH;+0:11]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Kinetic and Mössbauer studies on the mechanism of protocatechuic acid 4,5-oxygenase.Zabinski R, Münck E, Champion PM, Wood JM1972 Aug 155048285
Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions.Sugimoto K, Senda T, Aoshima H, Masai E, Fukuda M, Mitsui Y1999 Aug 1510467151