Information on EC 2.3.2.15 - glutathione gamma-glutamylcysteinyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.3.2.15
-
RECOMMENDED NAME
GeneOntology No.
glutathione gamma-glutamylcysteinyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glutathione + [Glu(-Cys)]n-Gly = Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
gamma-glutamylcysteinyl transfer
-
-
-
-
gamma-glutamylcysteinyl transfer
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
-
gamma-glutamylcysteinyl transfer
-
-
gamma-glutamylcysteinyl transfer
-
-
PATHWAY
KEGG Link
MetaCyc Link
phytochelatins biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
glutathione:poly(4-glutamyl-cysteinyl)glycine 4-glutamylcysteinyltransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
BjPCS1
-
-
gamma-glutamyl-cysteine transpeptidase
Q9S7Z3
-
gamma-glutamylcysteine dipeptidyl transpeptidase
-
-
-
-
gamma-glutamylcysteine transpeptidase
H2DFA2
-
gamma-glutamylcysteinyl dipeptidyl transpeptidase
-
-
gamma-glutamylcysteinyl transpeptidase
-
-
LjPCS1
Q2TSC7
-
LjPCS3
Q2QKL5
-
NsPCS
-
-
NsPCS
Nostoc sp. PCC7120
-
-
-
PC synthase
Q948S0
-
PC synthase
-
-
PC synthase
Nostoc sp. PCC7120
-
-
-
PC synthase
Q4QY91
-
PC synthase
Saccharomyces pombe
-
-
PCS
Arabidopsis thaliana Heyn.
-
-
-
PCS
-
-
PCS
Nostoc sp. PCC7120
-
-
-
PCS
Saccharomyces pombe
-
-
PCS
C7DSA3, C7DSA6, C7DSA8, Q1L734
-
PCS1
Q56VL5
isoform
PCS1
Q698X7
isoform
PCS1
H2DFA2
-
PCS2
F1KLT6
isoform
PCS2
B3FMV8
isoform
phytochelatin synthase
-
-
-
-
phytochelatin synthase
F1KLT6, Q56VL5
-
phytochelatin synthase
Q9S7Z3
-
phytochelatin synthase
Q948S0
-
phytochelatin synthase
-
-
phytochelatin synthase
-
-
phytochelatin synthase
E5GCW5
-
phytochelatin synthase
-
-
phytochelatin synthase
-
-
phytochelatin synthase
-
-
phytochelatin synthase
Q2QKL5, Q2TSC7
-
phytochelatin synthase
-
-
phytochelatin synthase
B3FMV8, Q698X7
-
phytochelatin synthase
-
-
phytochelatin synthase
Nostoc sp. PCC7120
-
-
-
phytochelatin synthase
-
-
phytochelatin synthase
Q4QY91
-
phytochelatin synthase
H2DFA2
-
phytochelatin synthase
Saccharomyces pombe
-
-
phytochelatin synthase
C7DSA3, C7DSA6, C7DSA8, Q1L734
-
phytochelatin synthase
Q4PJK2
-
phytochelatin synthase
Tetrahymena thermophila SB1969
Q4PJK2
-
-
phytochelatin synthase1
-
-
pseudo-phytochelatin synthase
Q4PJK2
biosynthetically inactive enzyme
pseudo-phytochelatin synthase
Tetrahymena thermophila SB1969
Q4PJK2
biosynthetically inactive enzyme
-
SrPCS
C7DSA3, C7DSA8, Q1L734
-
SrPCS1
Q1L734
isoform 1, produced by alternative splicing of the SrPCS pre-mRNA
SrPCS2
C7DSA6
isoform 2, produced by alternative splicing of the SrPCS pre-mRNA
SrPCS3
C7DSA3
isoform 3, produced by alternative splicing of the SrPCS pre-mRNA
SrPCS4
C7DSA8
isoform 4, produced by alternative splicing of the SrPCS pre-mRNA
TtpsiPCS
Q4PJK2
biosynthetically inactive enzyme
TtpsiPCS
Tetrahymena thermophila SB1969
Q4PJK2
biosynthetically inactive enzyme
-
CAS REGISTRY NUMBER
COMMENTARY
125390-02-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoform PCS1
UniProt
Manually annotated by BRENDA team
isoform PCS2
UniProt
Manually annotated by BRENDA team
ecotype Columbia
UniProt
Manually annotated by BRENDA team
ecotype Columbia; has a second gene (AtPCS2) encoding another functional phytochelatin synthase
-
-
Manually annotated by BRENDA team
ecotype Wassilewskija
-
-
Manually annotated by BRENDA team
strain Heyn.
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana Heyn.
strain Heyn.
-
-
Manually annotated by BRENDA team
L. cv. Vitasso
-
-
Manually annotated by BRENDA team
Caenorhabditis elegans N2
strain N2
Uniprot
Manually annotated by BRENDA team
cultivar Goldensun
-
-
Manually annotated by BRENDA team
sacred lotus, cultivar Donghe
-
-
Manually annotated by BRENDA team
cv. Bright Yellow-2
-
-
Manually annotated by BRENDA team
isoform PCS1; formerly Thlaspi caerulescens
UniProt
Manually annotated by BRENDA team
isoform PCS2; formerly Thlaspi caerulescens
UniProt
Manually annotated by BRENDA team
; PCC7120
-
-
Manually annotated by BRENDA team
Nostoc sp. PCC7120
PCC7120
-
-
Manually annotated by BRENDA team
isoform PCS1; birch-leaf pear
UniProt
Manually annotated by BRENDA team
Saccharomyces pombe
-
-
-
Manually annotated by BRENDA team
truncated
UniProt
Manually annotated by BRENDA team
strain Wib.
-
-
Manually annotated by BRENDA team
Silene vulgaris Wib.
strain Wib.
-
-
Manually annotated by BRENDA team
tomato, strain Mill. cv. VFNT-Cherry
-
-
Manually annotated by BRENDA team
strain SB1969
UniProt
Manually annotated by BRENDA team
Tetrahymena thermophila SB1969
strain SB1969
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
phytochelatins play an important role in detoxification of heavy metals in plants; phytochelatins play an important role in detoxification of heavy metals in plants; phytochelatins play an important role in detoxification of heavy metals in plants; phytochelatins play an important role in detoxification of heavy metals in plants
physiological function
-
the enzyme is involved in the response of Nelumbo nucifera to cadmium stress
physiological function
-
yeast cells producing both Arabidopsis thaliana phytochelatin synthase and cysteine desulfhydrase show a higher level of arsenic accumulation than a simple cumulative effect of expressing both enzymes confirming the importance of coordinated action of hydrogen sulfide and phytochelatins in the overall bioaccumulation of arsenic
physiological function
-
at CdSO4 concentrations up to 0.06 mM that have no or only slightly toxic effects on the growth of wild type Arabidopsis seedlings, phytochelatin synthase(PCS1) overexpression results in a decrease in Cd tolerance compared with the wild type, as mainly revealed by a reduced root growth. At higher Cd concentrations (0.09-0.18 mM CdSO4) toxic to wild type seedlings (as manifested by a significant decrease in fresh weight and root growth as well as by foliar chlorosis) PCS1 overexpression confers an increase in Cd tolerance
physiological function
-
enzyme expression leads to increased Cd2+ accumulation and enhanced metal tolerance. Enzyme overexpression leads to an increase in the antioxidative activity and a decrease in the oxidative damage induced by Cd toxicity
physiological function
E5GCW5
enhanced metal (Cd2+ and As5+) accumulation is due to post-translational activation of the enzyme in the presence of Cd2+ ion
physiological function
-, F1KLT6, Q56VL5
the enzyme is involved in cellular cadmium tolerance; the enzyme is involved in cellular cadmium tolerance
physiological function
B3FMV8, -, Q698X7
the enzyme is involved in cellular cadmium tolerance; the enzyme is involved in cellular cadmium tolerance
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
show the reaction diagram
Silene vulgaris, Arabidopsis thaliana Heyn., Silene vulgaris Wib.
-
-
-
-
?
glutathione + [Glu(-Cys)]n -Gly
Gly + [Glu(-Cys)]n+1 -Gly
show the reaction diagram
Q9S7Z3
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
Q9S7Z3
-
-
-
?
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
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
Saccharomyces pombe
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
Q948S0
-
-
-
?
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
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
-
-
-
?
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
-, F1KLT6, Q56VL5
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
B3FMV8, -, Q698X7
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
H2DFA2
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
E5GCW5
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
-
n = 2-5
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
-
n = 2-11
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
n = 2-5
-
-
-
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
n = 2-11, cellular functions are formation of heavy-metal binding peptides and degradation of glutathione-S-conjugates
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
G5ECE4
critical for heavy metal tolerance
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
critical for heavy metal tolerance
-
-
-
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
synthesis of photochelatin
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
Nostoc sp. PCC7120
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
Arabidopsis thaliana Heyn.
-
-
n = 2-11
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
Arabidopsis thaliana Heyn.
-
n = 2-11, cellular functions are formation of heavy-metal binding peptides and degradation of glutathione-S-conjugates
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
Silene vulgaris Wib.
-
-
-
?
monobromobimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-monobromobimane-Cys-Gly
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
Arabidopsis thaliana, Arabidopsis thaliana Heyn.
-
-
-
-
?
monochlorobimane + ?
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
despite constitutive expression of the enzyme during most stages of plant development, Brassica juncea may react to prolonged exposure to Cd2+ with an increase of phytochelatin synthase protein in leaves
-
-
-
additional information
?
-
-
the presence of VdCl2 activates phytochelatin synthase and induces the synthesis of substantial amounts of phytochelatins
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
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
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
-
-
-
?
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
-
n = 2-5
-
-
-
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
n = 2-11, cellular functions are formation of heavy-metal binding peptides and degradation of glutathione-S-conjugates
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
G5ECE4
critical for heavy metal tolerance
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
-
critical for heavy metal tolerance
-
-
-
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
Arabidopsis thaliana Heyn.
-
n = 2-11, cellular functions are formation of heavy-metal binding peptides and degradation of glutathione-S-conjugates
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
show the reaction diagram
Silene vulgaris Wib.
-
-
-
-
?
additional information
?
-
-
despite constitutive expression of the enzyme during most stages of plant development, Brassica juncea may react to prolonged exposure to Cd2+ with an increase of phytochelatin synthase protein in leaves
-
-
-
additional information
?
-
-
the presence of VdCl2 activates phytochelatin synthase and induces the synthesis of substantial amounts of phytochelatins
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ag+
-
activation
Ag+
-
activation
Ag+
-
activation
Ag+
-
activation
Ag+
-
activator
Al3+
-, Q2QKL5, Q2TSC7
activation of LjPCS1; activation of LjPCS3
As3+
-
activation
AsO43-
-
activation, wild-type and AtPCS2-enzyme
AsO43-
-
activator
Au+
-
activation
Bi3+
-
activation
Ca2+
-
enhanced activity, in the presence of Cd2+
Cd2+
-
activation; strongly dependent, optimal concentration 0.03 mM
Cd2+
-
activation; best at 0.4 mM
Cd2+
-
activation; under 0.085 mM CdCl2 stress for 3d, 1.3- to 2.1-fold increase when compared with wild-type
Cd2+
-
activation; best at 0.05 mM
Cd2+
-
activation; activation of AtPCS2-enzyme
Cd2+
-
activation
Cd2+
-
activation; best at 0.5 mM
Cd2+
-
activation
Cd2+
-
required, 0.5 mM
Cd2+
-
activation
Cd2+
-
most potent activator
Cd2+
Q948S0
-
Cd2+
-
-
Cd2+
-
enhanced activity
Cd2+
-
enhanced activity
Cd2+
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
-
Cd2+
-
the enzyme possesses two Cd2+ binding sites, Cd2+ binds to one of these sites to activate the enzyme. In the presence of 0.01 mM Cd2+, activity increases and reaches the maximum rate with an increase in GSH concentration up to 15 mM
Cd2+
-
the enzyme is stimulated by more than 2fold by free Cd2+ concentrations of 0.00035-0.001 mM
Cd2+
-, F1KLT6, Q56VL5
Cd2+ activates the enzyme. Extremely efficient alternative cadmium sequestration pathways in leaves of cadmium hyperaccumulators prevent activation of phytochelatin synthase by cadmium ions; Cd2+ activates the enzyme. Extremely efficient alternative cadmium sequestration pathways in leaves of cadmium hyperaccumulators prevent activation of phytochelatin synthase by cadmium ions
Cd2+
B3FMV8, -, Q698X7
Cd2+ activates the enzyme. Extremely efficient alternative cadmium sequestration pathways in leaves of cadmium hyperaccumulators prevent activation of phytochelatin synthase by cadmium ions; Cd2+ activates the enzyme. Extremely efficient alternative cadmium sequestration pathways in leaves of cadmium hyperaccumulators prevent activation of phytochelatin synthase by cadmium ions
Co2+
-
activation
Co2+
-
activation
Cu2+
-
activation; optimal at 0.04 mM, can replace Cd2+
Cu2+
-
activation
Cu2+
-
activation
Cu2+
-
activation
Cu2+
-
activation
Cu2+
-
activation
Cu2+
-
activator
Cu2+
-, Q2QKL5, Q2TSC7
activation of LjPCS3
Fe2+
-
activation
Fe2+
-, Q2QKL5, Q2TSC7
activation of LjPCS1; activation of LjPCS3
Hg2+
-
activation
Hg2+
-
activation
Hg2+
-
activation
Hg2+
-
activation
Hg2+
-
activator
Hg2+
-, Q2QKL5, Q2TSC7
activation of LjPCS3
KH2AsO4
-, Q2QKL5, Q2TSC7
activation of LjPCS3
La3+
-
enhanced activity, in the presence of Cd2+
Ni2+
-
activation
Pb2+
-
activation
Pb2+
-
activation
Pb2+
-
activation
Pb2+
-
activation
Pb2+
-
activator
Pb2+
-, Q2QKL5, Q2TSC7
activation of LjPCS3; best activator of LjPCS1 in the in vitro assay
Sb3+
-
activator
Zn2+
-
activation; optimal at 0.1 mM, can replace Cd2+
Zn2+
-
best at 0.2 mM
Zn2+
-
activation
Zn2+
-
activation
Zn2+
-
activation
Zn2+
-
activation
Zn2+
-
activator
Zn2+
-, Q2QKL5, Q2TSC7
activation of LjPCS3
Mg2+
-
activation
additional information
-
free metal ions are not essential for catalysis
additional information
-
characterization of metal-binding site
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Cd2+
-
the enzyme also possesses a second Cd2+ binding site where Cd2+ binds to induce an inhibitory effect
Cd2+
-
the enzyme lacking the C-terminal domain is inhibited by 0.001-0.005 mM Cd2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5
-
bimane-glutathione
-
-
-
6.7
-
glutathione
-
-
7.5
-
glutathione
-
-
7.7
-
glutathione
-
-
8.6
-
glutathione
-
-
1.5
-
monobromobimane-glutathione
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.09
-
-
10 ng/ml rAtPCS1
6.6
-
-
30 ng/ml rAtPCS1
12.6
-
-
50 ng/ml rAtPCS1
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6
-
-
activity assay
8
-
-
half maximal activity at pH 6.2 and 9.2
8
-
-
activity assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
activity assay
37
-
-
activity assay
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
47
-
half-maximal activity at 20C and 47C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9.4
-
H2DFA2
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
young, growing leaves, middle, fully expanded leaves or old, senescing leaves. Despite constitutive expression of the enzyme during most stages of plant development, Brassica juncea may react to prolonged exposure to CD2+ with an increase of phytochelatin synthase protein in leaves
Manually annotated by BRENDA team
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
-
Manually annotated by BRENDA team
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
-
Manually annotated by BRENDA team
H2DFA2
isoform PCS1 expression levels are higher in roots than in leaves and stems
Manually annotated by BRENDA team
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
-
Manually annotated by BRENDA team
H2DFA2
isoform PCS1 has a very low basal expression level in untreated whole seedlings
Manually annotated by BRENDA team
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
-
Manually annotated by BRENDA team
additional information
-
high expression in vascular tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Nostoc sp. (strain PCC 7120 / UTEX 2576)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
19800
-
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
theoretical
19900
-
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
theoretical
26000
-
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
theoretical
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
47000
-
Saccharomyces pombe
-
SDS-PAGE
52400
-
Q4PJK2, -
theoretical
55000
-
-
SDS-PAGE
55800
-
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
theoretical
56000
-
-
SDS-PAGE
56000
-
-
determined by SDS-PAGE and Western Blot analysis
56300
-
-
recombinant enzyme, SDS-PAGE
56300
-
-
AtPCS1, residues 1-485, theoretical, verified by SDS-PAGE and Western Blot analysis
56500
-
-
determined by SDS-PAGE
56900
-
-
calculated from sequence of cDNA
95000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 125480, calculated from amino acid sequence
?
-
x * 56500, SDS-PAGE
?
H2DFA2
x * 55000, calculated from amino acid sequence
?
-, F1KLT6, Q56VL5
x * 54000, calculated from amino acid sequence; x * 54000, calculated from amino acid sequence
?
B3FMV8, -, Q698X7
x * 54000, calculated from amino acid sequence; x * 54000, calculated from amino acid sequence
homotetramer
-
4 * 25000, SDS-PAGE, dimer also catalytically active
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
PCS1 expressed in Escherichia coli is phosphorylated at a Thr residue near its catalytic site
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
most stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-20
-
-
30% glycerol, 500 h, small activity decrease
4
-
-
50% activity after 6 h
4
-
-
50% activity after 140 h
22
-
-
50% activity after 34 h
35
-
-
50% activity after 0.5 h
35
-
-
50% activity after 0.5 h
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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
at 30% glycerol,m/v, stability enhancement
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 10 mM Tris-HCl, pH 8.0, 1 mM mercaptoethanol, 20% glycerol and 1% bovine serum albumin
-
-20C, best storage temperature
-
-20C, 10 mM Tris-HCl, pH 8.0, 10 mM 2-mercaptoethanol, 0.1% NaN3
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
on a Ni2+ affinity column
-
recombinant enzyme
-
using a HisTrap FF column
-
DEAE-Toyopearl column chromatography and HiTrap SP column chromatography; recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Saccharomyces cerevisiae strain BY4741; expressed in Saccharomyces cerevisiae strain BY4741
-, F1KLT6, Q56VL5
; 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
-
into the vector pET-28b for expression in Escherichia coli BL21 Rosetta DE3 pLysS cells
-
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 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
-
the plasmid pYES3-AtPCS1-FLAG is used for the transformation of Saccharomyces cerevisiae cells
-
transformed into Saccharomyces cerevisiae DTY167
-
truncated mutant enzymes
-
BjPCS1 is expressed in Escherichia coli
-
expressed in Schizosaccharomyces pombe strain SP27, a phytochelatin synthase knockout strain
-
into the binary plasmid vector pCB302 for introducing into Agrobacterium GV3101 strain, tobacco plants are transformed by the standard leaf disc method
-
transformed into Saccharomyces cerevisiae strain DTY67, hypersensitive to Cd2+-stress
G5ECE4
expressed in a Arabidopsis thaliana cad1-3 phytochelatin-deficient mutant and in Nicotiana tabacum cultivar Petit Havana
E5GCW5
expressed in Nicotiana tabacum and Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae
-
expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae. Yeast cells expressing LjPCS3 show increased in vivo tolerance to Cd
-, Q2QKL5, Q2TSC7
expressed in Arabidopsis thaliana via transformation with Agrobacterium tumefaciens strain EHA105
-
expressed in Saccharomyces cerevisiae strain BY4741; expressed in Saccharomyces cerevisiae strain BY4741
B3FMV8, -, Q698X7
expressed in Saccharomyces cerevisiae strain YK44 and Nicotiana tabacum strain NC89
-
; expressed in Escherichia coli BL21(DE3) cells
-
expressed in Saccharomyces cerevisiae
-
into the pGEM-T easy vector for sequencing, into the vector pYES2 for expression in Saccharomyces cerevisiae cells; into the pGEM-T easy vector for sequencing, into the vector pYES2 for expression in Saccharomyces cerevisiae cells; into the pGEM-T easy vector for sequencing, into the vector pYES2 for expression in Saccharomyces cerevisiae cells; into the pGEM-T easy vector for sequencing, into the vector pYES2 for expression in Saccharomyces cerevisiae cells
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
with the TOPO TA Cloning kit for sequencing
Q4PJK2, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
there is no significant change in transcript accumulation of PCS1 following Cd2+ treatment
E5GCW5
the expression of the enzyme in leaves of Nelumbo nucifera is dramatically increased in response to cadmium (0.4 mM) treatment. In the root, enzyme expression initially raises slightly after exposure to Cd, but falls back after 1 h. When exposed to cadmium (0.1 mM) stress, Arabidopsis transgenic plants heterologous expressing the enzyme accumulate more cadmium when compared with wild type
-
enzyme expression increases gradually in the leaves when given a treatment of 0.1, 0.2 or 0.5 mM CdCl2 for 4 or 8 h
-
L-buthionine-sulfoximine can inhibit isoform PCS1 expression in roots, stems and leaves
H2DFA2
after 24 h of exposure to 0.02 mM CdSO4, CuSO4 or ZnSO4, isoform PCS1 expression increases significantly. The increases in roots are in order of 4.34fold, 0.26fold or 2.82fold after exposure to CdSO4, CuSO4 or ZnSO4, respectively. Reduced L-glutathione stimulates isoform PCS1 expression in roots, stems and leaves (1.45-2.85fold)
H2DFA2
up-regulated under cadmium stress conditions
Q4PJK2, -
up-regulated under cadmium stress conditions
Tetrahymena thermophila SB1969
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
R183a
-
AtPCS1 mutant, Arg183 is critical to the activity of PCS; AtPCS1-N mutant, Arg183 is critical to the activity of PCS
T49A
-
AtPCS1 mutant, Thr49 is the only residue to be phosphorylated; AtPCS1-N mutant, Thr49 is the only residue to be phosphorylated
Y55A
-
AtPCS1 mutant; AtPCS1-N mutant
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
biotechnology
C7DSA3, C7DSA6, C7DSA8, Q1L734, -
SrPCS1 has potential applications in genetic engineering of plants for enhancing heavy metal tolerance and phytoremediation of contaminated soils; SrPCS3 has potential applications in genetic engineering of plants for enhancing heavy metal tolerance and phytoremediation of contaminated soils