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2.3.2.15: glutathione gamma-glutamylcysteinyltransferase

This is an abbreviated version!
For detailed information about glutathione gamma-glutamylcysteinyltransferase, go to the full flat file.

Word Map on EC 2.3.2.15

Reaction

glutathione
+
[Glu(-Cys)]n-Gly
=
Gly
+
[Glu(-Cys)]n+1-Gly

Synonyms

AdPCS1, AdPCS2, AdPCS3, alr0975, AtPCS, AtPCS1, AtPCS2, AtPCSI, BjPCS1, CaPCS1, CaPCS2, CePCS, DaPCS1, gamma-EC dipeptidyl(trans)peptidase, gamma-glutamyl-cysteine transpeptidase, gamma-glutamylcysteine dipeptidyl transpeptidase, gamma-glutamylcysteine transpeptidase, gamma-glutamylcysteinyl dipeptidyl transpeptidase, gamma-glutamylcysteinyl transpeptidase, glutathione gamma-glutamylcysteinyltransferase, LjPCS1, LjPCS3, MnPCS1, MnPCS2, NsPCS, OsPCS1, OsPCS15, OsPCS1a, OsPCS1b, OsPCS1c, OsPCS1full, OsPCS2, OsPCS5, PC synthase, PCS, PCS1, PCS15, PCS2, PCS5, phytochelatin synthase, phytochelatin synthase 1, phytochelatin synthase 2, phytochelatin synthase1, pPhytochelatin synthase, pseudo-phytochelatin synthase, SrPCS, SrPCS1, SrPCS2, SrPCS3, SrPCS4, TtpsiPCS

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.15 glutathione gamma-glutamylcysteinyltransferase

Engineering

Engineering on EC 2.3.2.15 - glutathione gamma-glutamylcysteinyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A182G/A282V/G329S
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
A59V
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
C109A
-
mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C109S
-
mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C109Y
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
C113A
-
mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C113S
-
mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C56S
-
mutation abolishes Cd2+ tolerance observed with wild-type enzyme, causes negligible intracellular phytochelatin accumulation
C90A
-
mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C90S
-
mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C91A
-
mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C91S
-
mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C91S/A199S
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
D180A
-
the mutation abolishes Cd2+ tolerance and phytocelatin synthetic activity
D71N
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
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
DELTA1-373
almost as stable and biosynthetically active (in the presence of cadmium) as the full-length enzyme
DELTA222-485
truncation mutant is fulla sufficient for phytochelatin synthesis. The fragment may be insufficient to maintain the active form of the enzyme stably in vitro
E52K
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
F83C/N170D
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
H162A
-
the mutation abolishes Cd2+ tolerance and phytocelatin synthetic activity
Q48R/C144Y/G168S/W280R
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
R183a
R74H/S230C/L250R
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
S51T/N143I/N170I/H220R
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
S60C/S202I
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
T123R/F163I
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
T139P
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
V181G
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
V97C
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
V97L
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
Y186C
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
additional information