EC number:2.3.2.15

Enzyme

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EC Tree
     2. Transferases
        2.3 Acyltransferases
            2.3.2 Aminoacyltransferases
ID:2.3.2.15
Description:Glutathione gamma-glutamylcysteinyltransferase.
Alternative Name: Phytochelatin synthase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.2.15
BRENDA Enzyme Link: BRENDA 2.3.2.15
KEGG Enzyme Link: KEGG2.3.2.15
BioCyc Enzyme Link: BioCyc 2.3.2.15
ExPASy Enzyme Link: ExPASy2.3.2.15
EC2PDB Enzyme Link: EC2PDB 2.3.2.15
ExplorEnz Enzyme Link: ExplorEnz 2.3.2.15
PRIAM enzyme-specific profiles Link: PRIAM 2.3.2.15
IntEnz Enzyme Link: IntEnz 2.3.2.15
MEDLINE Enzyme Link: MEDLINE 2.3.2.15

EC number:2.3.2.15

MSA:

2.3.2.15;
Phylogenetic Tree:

2.3.2.15;
Uniprot:
M-CSA:
RHEA:17917 [Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[NH;+0:4]-[C;H0;+0:5](=[*:6])-[*:7]>>[*:3]-[NH2;+0:4].[*:1]-[NH;+0:2]-[C;H0;+0:5](=[*:6])-[*:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase).Grill E, Löffler S, Winnacker EL, Zenk MH1989 Sep16594069