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Literature summary extracted from

  • Rea, P.A.
    Phytochelatin synthase: of a protease a peptide polymerase made (2012), Physiol. Plant., 145, 154-164.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.15 expressed in Saccharomyces cerevisiae Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.15 D180A the mutation abolishes Cd2+ tolerance and phytocelatin synthetic activity Arabidopsis thaliana
2.3.2.15 H162A the mutation abolishes Cd2+ tolerance and phytocelatin synthetic activity Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.15 Cd2+ the enzyme lacking the C-terminal domain is inhibited by 0.001-0.005 mM Cd2+ Arabidopsis thaliana

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.2.15 Cd2+ the enzyme is stimulated by more than 2fold by free Cd2+ concentrations of 0.00035-0.001 mM Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.15 Arabidopsis thaliana
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.15 glutathione + [Glu(-Cys)]n-Gly
-
 Arabidopsis thaliana Gly + [Glu(-Cys)]n+1-Gly
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.15 PC synthase
-
 Arabidopsis thaliana
2.3.2.15 PCS1
-
 Arabidopsis thaliana
2.3.2.15 phytochelatin synthase
-
 Arabidopsis thaliana