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Literature summary for 2.3.2.15 extracted from

  • Ruotolo, R.; Peracchi, A.; Bolchi, A.; Infusini, G.; Amoresano, A.; Ottonello, S.
    Domain organization of phytochelatin synthase: functional properties of truncated enzyme species identified by limited proteolysis (2004), J. Biol. Chem., 279, 14686-14693.
    View publication on PubMed
Search for more literature for 2.3.2.15

Cloned(Commentary)

Cloned (Comment) Organism
truncated mutant enzymes Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
DELTA1-284 biosynthetically active in the presence of cadmium ions and supporting phytochelatin formation at a rate that is only about 5fold lower than that of full-length AtPCS1. The loss of the C-terminal region substantially decreases the thermal stability of the enzyme and impairs phytochelatin formation in the presence of certain heavy metals Arabidopsis thaliana
DELTA1-373 almost as stable and biosynthetically active (in the presence of cadmium) as the full-length enzyme Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9S7Z3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Arabidopsis thaliana

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
AtPCS1
-
 Arabidopsis thaliana

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
42
-
 40 min, wild-type enzyme loses about 40% of its activity, mutant enzyme DELTA1-284 loses about 90% of its initial activity, mutant enzyme DELTA1-373 loses about 60% of ist initial activity Arabidopsis thaliana