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Information on EC 2.3.2.15 - glutathione gamma-glutamylcysteinyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9S7Z3

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     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.15 glutathione gamma-glutamylcysteinyltransferase
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Select one or more organisms in this record:
This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9S7Z3 not found.
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Arabidopsis thaliana
Synonyms
AtPCS, AtPCS1, AtPCSI, BjPCS1, CePCS, gamma-glutamyl-cysteine transpeptidase, gamma-glutamylcysteine dipeptidyl transpeptidase, gamma-glutamylcysteine transpeptidase, gamma-glutamylcysteinyl dipeptidyl transpeptidase, gamma-glutamylcysteinyl transpeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AtPCS1
gamma-glutamyl-cysteine transpeptidase
290284
-
gamma-glutamylcysteine dipeptidyl transpeptidase
-
-
-
-
gamma-glutamylcysteinyl dipeptidyl transpeptidase
302
-
gamma-glutamylcysteinyl transpeptidase
302
-
phytochelatin synthase
phytochelatin synthase 1
290284
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-glutamylcysteinyl transfer
-
-
gamma-glutamylcysteinyl transfer
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
glutathione:poly(4-glutamyl-cysteinyl)glycine 4-glutamylcysteinyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
125390-02-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
-
-
-
?
acetamido-fluorescein-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-acetamido-fluorescein-Cys-Gly
show the reaction diagram
-
-
-
-
?
benzyl-glutathione + [Glu(-Cys)]n Gly
Gly + [Glu(-Cys)]n-Glu-S-benzyl-Cys-Gly
show the reaction diagram
-
-
-
-
?
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
show the reaction diagram
-
-
-
-
?
glutathione + [Glu(-Cys)]n -Gly
Gly + [Glu(-Cys)]n+1 -Gly
show the reaction diagram
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
monochlorobimane + ?
?
show the reaction diagram
-
-
-
-
?
nitrobenzyl-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-nitrobenzyl-Cys-Gly
show the reaction diagram
-
-
-
-
?
S-butylglutathione + [Glu(-Cys)]n Gly
Gly + [Glu(-Cys)]n-Glu-S-butyl-Cys-Gly
show the reaction diagram
-
-
-
-
?
S-ethylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-ethyl-Cys-Gly
show the reaction diagram
-
-
-
-
?
S-hexylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-hexyl-Cys-Gly
show the reaction diagram
-
-
-
-
?
S-methylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-methyl-Cys-Gly
show the reaction diagram
-
n = 2,3
-
-
?
S-propylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-propyl-Cys-Gly
show the reaction diagram
-
-
-
-
?
uracil-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-uracil-Cys-Gly
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the presence of VdCl2 activates phytochelatin synthase and induces the synthesis of substantial amounts of phytochelatins
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
additional information
?
-
-
the presence of VdCl2 activates phytochelatin synthase and induces the synthesis of substantial amounts of phytochelatins
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AsO43-
Co2+
-
activation
Mg2+
-
activation
Ni2+
-
activation
Sb3+
-
activator
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cd2+
-
the activity of PCS requires Cd and is enhanced by protein phosphorylation
GSH
-
the maximal activity is attained at GSH concentrations around 10 and 15 mM when the enzyme is assayed in the presence of 0.005 and 0.01 mM total Cd2+, respectively
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.3
-
mutant enzyme Y186C, at pH 8.0 and 30°C
1.8
-
mutant enzyme C109Y, at pH 8.0 and 30°C
2.6
-
mutant enzyme T139P, at pH 8.0 and 30°C
2.8
-
mutant enzyme V181G, at pH 8.0 and 30°C; mutant enzyme V97C, at pH 8.0 and 30°C
2.9
-
mutant enzyme A59V, at pH 8.0 and 30°C
3.1
-
mutant enzyme F83C/N170D, at pH 8.0 and 30°C
3.2
-
mutant enzyme E52K, at pH 8.0 and 30°C
3.3
-
mutant enzyme S51T/N143I/N170I/H220R, at pH 8.0 and 30°C
3.6
-
mutant enzyme T123R/F163I, at pH 8.0 and 30°C
3.7
-
mutant enzyme R74H/S230C/L250R, at pH 8.0 and 30°C
4.09
-
10 ng/ml rAtPCS1
4.6
-
mutant enzyme C91S/A199S, at pH 8.0 and 30°C
4.8
-
mutant enzyme V97L, at pH 8.0 and 30°C
5
-
mutant enzyme Q48R/C144Y/G168S/W280R, at pH 8.0 and 30°C
5.1
-
mutant enzyme D71N, at pH 8.0 and 30°C
5.5
-
mutant enzyme A182G/A282V/G329S, at pH 8.0 and 30°C
5.9
-
mutant enzyme S60C/S202I, at pH 8.0 and 30°C
6.6
-
30 ng/ml rAtPCS1
12.6
-
50 ng/ml rAtPCS1
16.8
-
wild type enzyme, at pH 8.0 and 30°C
18.4
-
10 ng/ml rAtPCS1, 100 ng/ml bovine serum albumin, BSA
20.9
-
1 ng/ml rAtPCS1, 10000 ng/ml bovine serum albumin, BSA
24.9
-
100 ng/ml rAtPCS1
25.9
-
200 ng/ml rAtPCS1
30
-
10 ng/ml rAtPCS1, 10000 ng/ml bovine serum albumin, BSA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
activity assay
8
-
activity assay
8
-
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
activity assay
37
-
activity assay
35
-
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme binds, localizes, stores or sequesters heavy metals in plant cells
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
PCS1_ARATH
485
0
54475
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26700
-
AtPCS1-N, residues 1-221, theoretical, verified by SDS-PAGE and Western Blot analysis
31400
-
AtPCS1-C, residues 222-485, theoretical, verified by SDS-PAGE and Western Blot analysis
55000
-
x * 55000, FLAG-tagged enzyme, SDS-PAGE
56300
-
AtPCS1, residues 1-485, theoretical, verified by SDS-PAGE and Western Blot analysis
56500
-
determined by SDS-PAGE
55000
-
SDS-PAGE
56000
56300
-
recombinant enzyme, SDS-PAGE
56500
-
x * 56500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 55000, FLAG-tagged enzyme, SDS-PAGE
?
-
x * 56500, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
PCS1 expressed in Escherichia coli is phosphorylated at a Thr residue near its catalytic site
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
C109Y
-
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
C91S/A199S
-
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
D71N
-
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
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
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
-
AtPCS1 mutant, Arg183 is critical to the activity of PCS; AtPCS1-N mutant, Arg183 is critical to the activity of PCS
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
T49A
-
AtPCS1 mutant, Thr49 is the only residue to be phosphorylated; AtPCS1-N mutant, Thr49 is the only residue to be phosphorylated
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
Y55A
-
AtPCS1 mutant; AtPCS1-N mutant
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
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
D180A
-
the mutation abolishes Cd2+ tolerance and phytocelatin synthetic activity
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
H162A
-
the mutation abolishes Cd2+ tolerance and phytocelatin synthetic activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM Tris-HCl, pH 8.0, 1 mM mercaptoethanol, 20% glycerol and 1% bovine serum albumin
-
-20°C, best storage temperature
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
on a Ni2+ affinity column
-
using a HisTrap FF column
-
DEAE-Toyopearl column chromatography, HiTrap SP column chromatography, and Hitrap Q sepharose column chromatography; recombinant enzyme
-
Ni2+ affinity column chromatography and HisTrap HP column chromatography
-
recombinant enzyme
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells and Saccharomyces cerevisiae strain TY167
-
into the vector pET-28b for expression in Escherichia coli BL21 Rosetta DE3 pLysS cells
-
the coding sequences of full-length PCS1, PCS-N, residues 1-221, and PCS-C, residues 222-485, are cloned into the vector pGEM-T-Easy and subsequently into pET28b for expression in Escherichia coli BL21DE3 cells
-
; expressed in Escherichia coli BL21(DE3) cells
-
AtPCS2-gene expressed in Saccharomyces cerevisiae strain INVSc1; AtPCS2-gene expressed in Schizosaccharomyces pombe strain FY254, a phytochelatin synthase knockout strain
-
expressed in Brassica juncea
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 Rosetta (DE3) pLysS cells
-
expressed in Nicotiana tabacum; overexpression both in wild-type and rolB-transformed Nicotiana tabacum. Increase in Cd2+ tolerance and accumulation in the overexpressing plants is directly related to the availability of reduced glutathione, while overexpression of phytochelatin synthase does not enhance long distance root-to shoot Cd2+ transport
-
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae strain BY4742
-
expression in Escherichia coli and Saccharomyces cerevisiae to enhance tolerance to toxicity of cadmium ion
-
expression in Mesorhizobium huakuii subsp. rengei B3. The PCS(At) gene is expressed under the control of the nifH promoter, which regulates the nodule-specific expression of nifH gene. Expression of the PCS(At) gene in Mesorhizobium huakuii subsp. rengei B3 increases the ability of cells to bind Cd2+ approximately 9fold to 19fold
-
fused to a C-terminal Flag epitope; heterologously expressed in Escherichia coli
-
fused to a C-terminal Flag epitope; transformed into Saccharomyces cerevisiae DTY167
-
heterologous expression of AtPCS1-FLAG in Saccharomyces cerevisiae
-
heterologously expressed in Escherichia coli
-
into the binary plasmid vector pCB302 for introducing into Agrobacterium GV3101 strain, tobacco plants are transformed by the standard leaf disc method
-
overexpressed in transgenic Arabidopsis thaliana
-
overexpression in Arabidopsis from a strong constitutive Arabidopsis actin regulatory sequence (A2), the A2::AtPCS1 plants are highly resistant to arsenic, accumulating 20-100times more biomass on 0.25 and 0.3 mM arsenate than wild-type, however, they are hypersensitive to Cd(II). After exposure to cadmium and arsenic, the overall accumulation of thiol-peptides increases to 10fold higher levels in the A2::AtPCS1 plants compared with wild-type
-
overexpression of AtPCS1 in transgenic Arabidopsis. Transgenic plants with a relatively high level of expression of the 35S::AtPCS1 transgene does not result in higher Cd tolerance, but rather show higher sensitivity to Cd under some conditions. Transgenic plants showing a relatively lower level of expression of the 35S::AtPCS1 transgene show increased accumulation and tolerance of Cd compared to wild-type plants
-
the plasmid pYES3-AtPCS1-FLAG is used for the transformation of Saccharomyces cerevisiae cells
-
transformed into Saccharomyces cerevisiae DTY167
-
truncated mutant enzymes
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
a HPLC method for the analysis of the activity of phytochelatin synthase is developed
biotechnology
-
plastid targeting of PCS
environmental protection
-
yeast cells expressing AtPCS can be used as an inexpensive sorbent for the removal of toxic arsenic
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beck, A.; Lendzian, K.; Oven, M.; Christmann, A.; Grill, E.
Phytochelatin synthase catalyzes key step in turnover of glutathione conjugates
Phytochemistry
62
423-431
2003
Arabidopsis thaliana, Arabidopsis thaliana Heyn., Silene vulgaris, Silene vulgaris Wib.
Manually annotated by BRENDA team
Lee, S.; Moon, J.S.; Ko, T.S.; Petros, D.; Goldsbrough, P.B.; Korban, S.S.
Overexpression of Arabidopsis phytochelatin synthase paradoxically leads to hypersensitivity to cadmium stress
Plant Physiol.
131
656-663
2003
Arabidopsis thaliana
Manually annotated by BRENDA team
Sauge-Merle, S.; Cuine, S.; Carrier, P.; Lecomte-Pradines, C.; Luu, D.T.; Peltier, G.
Enhanced toxic metal accumulation in engineered bacterial cells expressing Arabidopsis thaliana phytochelatin synthase
Appl. Environ. Microbiol.
69
490-494
2003
Arabidopsis thaliana, Arabidopsis thaliana (Q9S7Z3)
Manually annotated by BRENDA team
Lee, S.; Moon, J.S.; Domier, L.L.; Korban, S.S.
Molecular characterization of phytochelatin synthase expression in transgenic Arabidopsis
Plant Physiol. Biochem.
40
727-733
2002
Arabidopsis thaliana
-
Manually annotated by BRENDA team
Cazale, A.C.; Clemens, S.
Arabidopsis thaliana expresses a second functional phytochelatin synthase
FEBS Lett.
507
215-219
2001
Arabidopsis thaliana
Manually annotated by BRENDA team
Vatamaniuk, O.K.; Mari, S.; Lu, Y.P.; Rea, P.A.
Mechanism of heavy metal ion activation of phytochelatin (PC) synthase: blocked thiols are sufficient for PC synthase-catalyzed transpeptidation of glutathione and related thiol peptides
J. Biol. Chem.
275
31451-31459
2000
Arabidopsis thaliana
Manually annotated by BRENDA team
Vatamaniuk, O.K.; Mari, S.; Lu, Y.P.; Rea, P.A.
AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution
Proc. Natl. Acad. Sci. USA
96
7110-7115
1999
Arabidopsis thaliana, Arabidopsis thaliana (Q9S7Z3)
Manually annotated by BRENDA team
Sriprang, R.; Hayashi, M.; Ono, H.; Takagi, M.; Hirata, K.; Murooka, Y.
Enhanced accumulation of Cd2+ by a Mesorhizobium sp. transformed with a gene from Arabidopsis thaliana coding for phytochelatin synthase
Appl. Environ. Microbiol.
69
1791-1796
2003
Arabidopsis thaliana
Manually annotated by BRENDA team
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
J. Biol. Chem.
279
14686-14693
2004
Arabidopsis thaliana (Q9S7Z3)
Manually annotated by BRENDA team
Vatamaniuk, O.K.; Mari, S.; Lang, A.; Chalasani, S.; Demkiv, L.O.; Rea, P.A.
Phytochelatin synthase, a dipeptidyltransferase that undergoes multisite acylation with gamma-glutamylcysteine during catalysis: stoichiometric and site-directed mutagenic analysis of Arabidopsis thaliana PCS1-catalyzed phytochelatin synthesis
J. Biol. Chem.
279
22449-22460
2004
Arabidopsis thaliana
Manually annotated by BRENDA team
Li, Y.; Dhankher, O.P.; Carreira, L.; Lee, D.; Chen, A.; Schroeder, J.I.; Balish, R.S.; Meagher, R.B.
Overexpression of phytochelatin synthase in Arabidopsis leads to enhanced arsenic tolerance and cadmium hypersensitivity
Plant Cell Physiol.
45
1787-1797
2004
Arabidopsis thaliana
Manually annotated by BRENDA team
Lee, S.; Petros, D.; Moon, J.S.; Ko, T.S.; Goldsbrough, P.B.; Korban, S.S.
Higher levels of ectopic expression of Arabidopsis phytochelatin synthase do not lead to increased cadmium tolerance and accumulation
Plant Physiol. Biochem.
41
903-910
2003
Arabidopsis thaliana
-
Manually annotated by BRENDA team
Maier, T.; Yu, C.; Kullertz, G.; Clemens, S.
Localization and functional characterization of metal-binding sites in phytochelatin synthases
Planta
218
300-308
2003
Arabidopsis thaliana, Schizosaccharomyces pombe
Manually annotated by BRENDA team
Tsuji, N.; Nishikori, S.; Iwabe, O.; Matsumoto, S.; Shiraki, K.; Miyasaka, H.; Takagi, M.; Miyamoto, K.; Hirata, K.
Comparative analysis of the two-step reaction catalyzed by prokaryotic and eukaryotic phytochelatin synthase by an ion-pair liquid chromatography assay
Planta
222
181-191
2005
Arabidopsis thaliana (Q9S7Z3), Nostoc sp.
Manually annotated by BRENDA team
Pomponi, M.; Censi, V.; Di Girolamo, V.; De Paolis, A.; di Toppi, L.S.; Aromolo, R.; Costantino, P.; Cardarelli, M.
Overexpression of Arabidopsis phytochelatin synthase in tobacco plants enhances Cd(2+) tolerance and accumulation but not translocation to the shoot
Planta
223
180-190
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Matsumoto, S.; Shiraki, K.; Tsuji, N.; Hirata, K.; Miyamoto, K.; Takagi, M.
Functional analysis of phytochelatin synthase from Arabidopsis thaliana and its expression in Escherichia coli and Saccharomyces cerevisiae
Sci. Tech. Adv. Mater.
5
377-381
2004
Arabidopsis thaliana
-
Manually annotated by BRENDA team
Picault, N.; Cazale, A.C.; Beyly, A.; Cuine, S.; Carrier, P.; Luu, D.T.; Forestier, C.; Peltier, G.
Chloroplast targeting of phytochelatin synthase in Arabidopsis: effects onheavy metal tolerance and accumulation
Biochimie
88
1743-1750
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Clemens, S.
Evolution and function of phytochelatin synthases
J. Plant Physiol.
163
319-332
2006
Arabidopsis thaliana, Athyrium yokoscense (Q948S0), Phaeodactylum tricornutum, Pteris vittata (Q4QY91), Saccharomyces pombe
Manually annotated by BRENDA team
Blum, R.; Beck, A.; Korte, A.; Stengel, A.; Letzel, T.; Lendzian, K.; Grill, E.
Function of phytochelatin synthase in catabolism of glutathione-conjugates
Plant J.
49
740-749
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Gasic, K.; Korban, S.S.
Expression of Arabidopsis phytochelatin synthase in Indian mustard (Brassica juncea) plants enhances tolerance for Cd and Zn
Planta
225
1277-1285
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Singh, S.; Lee, W.; DaSilva, N.; Mulchandani, A.; Chen, W.
Enhanced arsenic accumulation by engineered yeast cells expressing Arabidopsis thaliana phytochelatin synthase
Biotechnol. Bioeng.
99
333-340
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Wang, H.; Wu, J.; Chia, J.; Yang, C.; Wu, Y.; Juang, R.
Phytochelatin synthase is regulated by protein phosphorylation at a threonine residue near its catalytic site
J. Agric. Food Chem.
57
7348-7355
2009
Arabidopsis thaliana (Q9S7Z3)
Manually annotated by BRENDA team
Wojas, S.; Clemens, S.; Hennig, J.; Sklodowska, A.; Kopera, E.; Schat, H.; Bal, W.; Antosiewicz, D.M.
Overexpression of phytochelatin synthase in tobacco: distinctive effects of AtPCS1 and CePCS genes on plant response to cadmium
J. Exp. Bot.
59
2205-2219
2008
Arabidopsis thaliana, Caenorhabditis elegans
Manually annotated by BRENDA team
Ogawa, S.; Yoshidomi, T.; Shirabe, T.; Yoshimura, E.
HPLC method for the determination of phytochelatin synthase activity specific for soft metal ion chelators
J. Inorg. Biochem.
104
442-445
2010
Arabidopsis thaliana, Arabidopsis thaliana (Q9S7Z3)
Manually annotated by BRENDA team
Tsai, S.L.; Singh, S.; Dasilva, N.A.; Chen, W.
Co-expression of Arabidopsis thaliana phytochelatin synthase and Treponema denticola cysteine desulfhydrase for enhanced arsenic accumulation
Biotechnol. Bioeng.
109
605-608
2012
Arabidopsis thaliana
Manually annotated by BRENDA team
Brunetti, P.; Zanella, L.; Proia, A.; De Paolis, A.; Falasca, G.; Altamura, M.M.; Sanita di Toppi, L.; Costantino, P.; Cardarelli, M.
Cadmium tolerance and phytochelatin content of Arabidopsis seedlings over-expressing the phytochelatin synthase gene AtPCS1
J. Exp. Bot.
62
5509-5519
2011
Arabidopsis thaliana
Manually annotated by BRENDA team
Ogawa, S.; Yoshidomi, T.; Yoshimura, E.
Cadmium(II)-stimulated enzyme activation of Arabidopsis thaliana phytochelatin synthase 1
J. Inorg. Biochem.
105
111-117
2011
Arabidopsis thaliana
Manually annotated by BRENDA team
Rea, P.A.
Phytochelatin synthase: of a protease a peptide polymerase made
Physiol. Plant.
145
154-164
2012
Arabidopsis thaliana
Manually annotated by BRENDA team
Cahoon, R.E.; Lutke, W.K.; Cameron, J.C.; Chen, S.; Lee, S.G.; Rivard, R.S.; Rea, P.A.; Jez, J.M.
Adaptive engineering of phytochelatin-based heavy metal tolerance
J. Biol. Chem.
290
17321-17330
2015
Arabidopsis thaliana, Arabidopsis thaliana (Q9S7Z3)
Manually annotated by BRENDA team
Nahar, N.; Rahman, A.; Mos, M.; Warzecha, T.; Ghosh, S.; Hossain, K.; Nawani, N.N.; Mandal, A.
In silico and in vivo studies of molecular structures and mechanisms of AtPCS1 protein involved in binding arsenite and/or cadmium in plant cells
J. Mol. Model.
20
2104
2014
Arabidopsis thaliana, Arabidopsis thaliana (Q9S7Z3)
Manually annotated by BRENDA team
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