Enzyme

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EC Tree
     3. Hydrolases
        3.8 Acting on halide bonds
            3.8.1 In carbon-halide compounds
ID:3.8.1.8
Description:Atrazine chlorohydrolase.
Cath: 3.20.20.140; 2.30.40.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.8.1.8
BRENDA Enzyme Link: BRENDA 3.8.1.8
KEGG Enzyme Link: KEGG3.8.1.8
BioCyc Enzyme Link: BioCyc 3.8.1.8
ExPASy Enzyme Link: ExPASy3.8.1.8
EC2PDB Enzyme Link: EC2PDB 3.8.1.8
ExplorEnz Enzyme Link: ExplorEnz 3.8.1.8
PRIAM enzyme-specific profiles Link: PRIAM 3.8.1.8
IntEnz Enzyme Link: IntEnz 3.8.1.8
MEDLINE Enzyme Link: MEDLINE 3.8.1.8
MSA:

3.8.1.8;

Phylogenetic Tree:

3.8.1.8;

Uniprot:
M-CSA:
RHEA:11312 atrazine + H2O = chloride + H(+) + hydroxyatrazine
RULE(radius=1) [*:1]:[c;H0;+0:2](:[*:3])-[Cl;H0;+0:4].[OH2;+0:5]>>[*:1]:[c;H0;+0:2](:[*:3])-[OH;+0:5].[Cl-;H0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Atrazine chlorohydrolase from Pseudomonas sp. strain ADP: gene sequence, enzyme purification, and protein characterization.de Souza ML, Sadowsky MJ, Wackett LP1996 Aug8759853
Cloning, characterization, and expression of a gene region from Pseudomonas sp. strain ADP involved in the dechlorination of atrazine.de Souza ML, Wackett LP, Boundy-Mills KL, Mandelbaum RT, Sadowsky MJ1995 Sep7574646
Atrazine chlorohydrolase from Pseudomonas sp. strain ADP is a metalloenzyme.Seffernick JL, McTavish H, Osborne JP, de Souza ML, Sadowsky MJ, Wackett LP2002 Dec 312450410
Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different.Seffernick JL, de Souza ML, Sadowsky MJ, Wackett LP2001 Apr11274097