Enzyme

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EC Tree
     3. Hydrolases
        3.7 Acting on carbon-carbon bonds
            3.7.1 In ketonic substances
ID:3.7.1.13
Description:2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.7.1.13
BRENDA Enzyme Link: BRENDA 3.7.1.13
KEGG Enzyme Link: KEGG3.7.1.13
BioCyc Enzyme Link: BioCyc 3.7.1.13
ExPASy Enzyme Link: ExPASy3.7.1.13
EC2PDB Enzyme Link: EC2PDB 3.7.1.13
ExplorEnz Enzyme Link: ExplorEnz 3.7.1.13
PRIAM enzyme-specific profiles Link: PRIAM 3.7.1.13
IntEnz Enzyme Link: IntEnz 3.7.1.13
MEDLINE Enzyme Link: MEDLINE 3.7.1.13
MSA:

3.7.1.13;

Phylogenetic Tree:

3.7.1.13;

Uniprot:
M-CSA:
RHEA:27870 (2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O = (2E)-2-hydroxypenta-2,4-dienoate + anthranilate + H(+)
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[CH;+0:4]=[*:5].[OH2;+0:6]>>[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6].[*:5]=[CH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and properties of 2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid hydrolase involved in microbial degradation of carbazole.Riddle RR, Gibbs PR, Willson RC, Benedik MJ2003 Mar12651123
Purification and characterization of meta-cleavage compound hydrolase from a carbazole degrader Pseudomonas resinovorans strain CA10.Nojiri H, Taira H, Iwata K, Morii K, Nam JW, Yoshida T, Habe H, Nakamura S, Shimizu K, Yamane H, Omori T2003 Jan12619671