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Information on EC 2.3.2.15 - glutathione gamma-glutamylcysteinyltransferase
for references in articles please use BRENDA:EC2.3.2.15
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.2 Aminoacyltransferases
2.3.2.15 glutathione gamma-glutamylcysteinyltransferase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 2.3.2.15
- phytochelatins
-
neurogenesis
- cadmium
-
subventricular
-
oligodendrocyte
-
neurospheres
-
hippocampal
- gsh
-
neurogenic
- arsenic
-
self-renewal
-
phytoremediation
- metallothioneins
- nestin
-
multipotent
-
asiii
-
subgranular
-
neuroblast
-
metalloid
-
cord-derived
- analysis
- agriculture
- biotechnology
- environmental protection
showSynonyms
nspcs, cepcs, phytochelatin synthase, atpcs1, ospcs1, ospcs2, atpcs2, atpcs, phytochelatin synthase 1, ljpcs1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtPCS
AtPCS1
AtPCS2
CaPCS1
CaPCS2
DaPCS1
gamma-glutamylcysteine dipeptidyl transpeptidase
-
-
-
-
NsPCS
OsPCS1
OsPCS2
PC synthase
PCS
PCS1
PCS2
phytochelatin synthase
phytochelatin synthase 1
phytochelatin synthase 2
pseudo-phytochelatin synthase
SrPCS1
isoform 1, produced by alternative splicing of the SrPCS pre-mRNA
SrPCS2
isoform 2, produced by alternative splicing of the SrPCS pre-mRNA
SrPCS3
isoform 3, produced by alternative splicing of the SrPCS pre-mRNA
SrPCS4
isoform 4, produced by alternative splicing of the SrPCS pre-mRNA
TtpsiPCS
phytochelatin synthase
-
-
-
-
phytochelatin synthase
-
-
pseudo-phytochelatin synthase
biosynthetically inactive enzyme
pseudo-phytochelatin synthase
biosynthetically inactive enzyme
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione + [Glu(-Cys)]n-Gly = Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
gamma-glutamylcysteinyl transfer
gamma-glutamylcysteinyl transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phytochelatins biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
glutathione:poly(4-glutamyl-cysteinyl)glycine 4-glutamylcysteinyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
125390-02-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetamido-fluorescein-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-acetamido-fluorescein-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
Cd2+-bis-glutathionate + [Glu(-Cys)]n-Gly
?
Substrates: -
Products: -
Products: -
?
metal-bis-glutathionate + [Glu(-Cys)]n-Gly
?
Substrates: Zn2+-bis-glutathionate is the best cosubstrate. The order of preference for the Me-GS2 substrate is Zn2+ > Cd2+ > Mn2+ > As5+ > As3+ > Cu2+ > Ag+
Products: -
Products: -
?
monobromobimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-monobromobimane-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
S-butylglutathione + [Glu(-Cys)]n Gly
Gly + [Glu(-Cys)]n-Glu-S-butyl-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
S-ethylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-ethyl-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
S-hexylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-hexyl-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
S-methylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-methyl-Cys-Gly
-
Substrates: n = 2,3
Products: -
Products: -
?
S-propylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-propyl-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
Zn2+-bis-glutathionate + [Glu(-Cys)]n-Gly
?
Substrates: Zn2+-bis-glutathionate is the best cosubstrate
Products: -
Products: -
?
benzyl-glutathione + [Glu(-Cys)]n Gly
Gly + [Glu(-Cys)]n-Glu-S-benzyl-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
benzyl-glutathione + [Glu(-Cys)]n Gly
Gly + [Glu(-Cys)]n-Glu-S-benzyl-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + Glu-Cys-Gly
Gly + [Glu(-Cys)]2-Gly
Substrates: -
Products: -
Products: -
?
glutathione + Glu-Cys-Gly
Gly + [Glu(-Cys)]2-Gly
K9S8X3
Substrates: -
Products: -
Products: -
?
glutathione + Glu-Cys-Gly
Gly + [Glu(-Cys)]2-Gly
Substrates: -
Products: -
Products: -
?
glutathione + Glu-Cys-Gly
Gly + [Glu(-Cys)]2-Gly
Substrates: -
Products: -
Products: -
?
glutathione + Glu-Cys-Gly
Gly + [Glu(-Cys)]2-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]2-Gly
Gly + [Glu(-Cys)]3-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]2-Gly
Gly + [Glu(-Cys)]3-Gly
K9S8X3
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]2-Gly
Gly + [Glu(-Cys)]3-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]2-Gly
Gly + [Glu(-Cys)]3-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]2-Gly
Gly + [Glu(-Cys)]3-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]3-Gly
Gly + [Glu(-Cys)]4-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]3-Gly
Gly + [Glu(-Cys)]4-Gly
K9S8X3
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]3-Gly
Gly + [Glu(-Cys)]4-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]3-Gly
Gly + [Glu(-Cys)]4-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n -Gly
Gly + [Glu(-Cys)]n+1 -Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n -Gly
Gly + [Glu(-Cys)]n+1 -Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: n = 2-11
Products: n = 2-11
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: n = 2-11
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: cellular functions are formation of heavy-metal binding peptides and degradation of glutathione-S-conjugates
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: synthesis of photochelatin
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: n = 2-11
Products: n = 2-11
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
G5ECE4
Substrates: critical for heavy metal tolerance
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
G5ECE4
Substrates: critical for heavy metal tolerance
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: n = 2-5
Products: n = 2-5
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: n = 2-5
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Saccharomyces pombe
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: critical for heavy metal tolerance
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
nitrobenzyl-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-nitrobenzyl-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
nitrobenzyl-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-nitrobenzyl-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
uracil-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-uracil-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
uracil-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-uracil-Cys-Gly
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the presence of VdCl2 activates phytochelatin synthase and induces the synthesis of substantial amounts of phytochelatins
Products: -
Products: -
?
additional information
?
-
Substrates: the PCS enzyme catalyzes transformation of GSH to give phytochelatins (PCs), it can effectively capture and enrich Cd2+ so that the generation and subsequent application process of CdS NPs is greatly improved
Products: -
Products: -
?
additional information
?
-
-
Substrates: the PCS enzyme catalyzes transformation of GSH to give phytochelatins (PCs), it can effectively capture and enrich Cd2+ so that the generation and subsequent application process of CdS NPs is greatly improved
Products: -
Products: -
?
additional information
?
-
Substrates: PC2 is the main polymerization product of PCS1, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
Substrates: PC2 is the main polymerization product of PCS1, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
Substrates: PC2 is the main polymerization product of PCS1, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
-
Substrates: PC2 is the main polymerization product of PCS1, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
Substrates: PC2 is the main polymerization product of PCS2, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
Substrates: PC2 is the main polymerization product of PCS2, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
Substrates: PC2 is the main polymerization product of PCS2, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
-
Substrates: PC2 is the main polymerization product of PCS2, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
Substrates: PC2 is the main polymerization product of PCS3, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
Substrates: PC2 is the main polymerization product of PCS3, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
Substrates: PC2 is the main polymerization product of PCS3, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
-
Substrates: PC2 is the main polymerization product of PCS3, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not use gamma-glutamylcysteine or phytochelatin2 as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not use gamma-glutamylcysteine or phytochelatin2 as substrate
Products: -
Products: -
?
additional information
?
-
K9S8X3
Substrates: enzyme produces phytochelatins up to the oligomer PC4. Synthesis of oligomers higher than PC2 requires the presence of Cd2+
Products: -
Products: -
-
additional information
?
-
Substrates: the presence of Cd2+, As3+ or As5+ is required for activity
Products: -
Products: -
-
additional information
?
-
Substrates: enzyme produces phytochelatins up to the oligomer PC4
Products: -
Products: -
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: n = 2-11
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: cellular functions are formation of heavy-metal binding peptides and degradation of glutathione-S-conjugates
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
G5ECE4
Substrates: critical for heavy metal tolerance
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
Products: -
Products: -
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
G5ECE4
Substrates: critical for heavy metal tolerance
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: n = 2-5
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Substrates: -
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: critical for heavy metal tolerance
Products: -
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glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
Substrates: -
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additional information
?
-
-
Substrates: the presence of VdCl2 activates phytochelatin synthase and induces the synthesis of substantial amounts of phytochelatins
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additional information
?
-
-
Substrates: 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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ag+
Al3+
As3+
AsO43-
Cd2+
Co2+
Cu2+
Fe2+
Hg2+
Pb2+
Zn2+
additional information
Ag+
up to 23fold activiation. Catalytic activity is enhanced by metal ions in the order Ag+ > Cd2+ > Cu2+ > Pb2+ > Hg2+ > Fe2+ > Zn2+
As3+
50fold activation at 0.05 mM, recombinant MBP-tagged isozyme PCS2
Cd2+
Cd2+ activates the enzyme. Extremely efficient alternative cadmium sequestration pathways in leaves of cadmium hyperaccumulators prevent activation of phytochelatin synthase by cadmium ions
Cd2+
-
under 0.085 mM CdCl2 stress for 3d, 1.3- to 2.1-fold increase when compared with wild-type
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+
-
activates the enzyme at 0.036-0.36 mM about 4-9fold. PCS activation is self-regulated, because its product poly(4-glutamyl-cysteinyl)glycine chelates Cd2+, and the reaction stops when free Cd2+ ions are no longer available. Cd2+ also activates the enzymes peptidase activity. Presence of PC2, PC3, and PC4 oligomers is evident in extracts from gametophytes exposed to Cd2+ for 7 days, determined by HPLC-ESI-MS-MS analysis
Cd2+
up to 12fold activation. Catalytic activity is enhanced by metal ions in the order Ag+ > Cd2+ > Cu2+ > Pb2+ > Hg2+ > Fe2+ > Zn2+
Cd2+
Cd2+ activates the enzyme. Extremely efficient alternative cadmium sequestration pathways in leaves of cadmium hyperaccumulators prevent activation of phytochelatin synthase by cadmium ions
Cd2+
70fold activation at 0.05 mM, recombinant MBP-tagged isozyme PCS2
Cu2+
catalytic activity is enhanced by metal ions in the order Ag+ > Cd2+ > Cu2+ > Pb2+ > Hg2+ > Fe2+ > Zn2+
Fe2+
catalytic activity is enhanced by metal ions in the order Ag+ > Cd2+ > Cu2+ > Pb2+ > Hg2+ > Fe2+ > Zn2+
Hg2+
catalytic activity is enhanced by metal ions in the order Ag+ > Cd2+ > Cu2+ > Pb2+ > Hg2+ > Fe2+ > Zn2+
Pb2+
catalytic activity is enhanced by metal ions in the order Ag+ > Cd2+ > Cu2+ > Pb2+ > Hg2+ > Fe2+ > Zn2+
Zn2+
catalytic activity is enhanced by metal ions in the order Ag+ > Cd2+ > Cu2+ > Pb2+ > Hg2+ > Fe2+ > Zn2+
additional information
-
free metal ions are not essential for catalysis
additional information
-
neither in vivo nor in vitro exposure to Zn2+ results in PCS activation, while Fe(II)/(III) and Cd2+ are able to activate enzyme PCS in vitro, as well as to induce phytochelatin (PC) accumulation in vivo. The enzyme activity depends on divalent cations, overview
additional information
OsPCS1 is more sensitive to activation by As than by cadmium, whereas OsPCS2 is more weakly activated by As than by cadmium
additional information
OsPCS1 is more sensitive to activation by As than by cadmium, whereas OsPCS2 is more weakly activated by As than by cadmium
additional information
isozyme OsPCS2 is more strongly activated by Cd2+ than by As3+, and it is vice versa for expression of OsPCS1
additional information
isozyme OsPCS2 is more strongly activated by Cd2+ than by As3+, and it is vice versa for expression of OsPCS1
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INHIBITOR
ORGANISM
UNIPROT
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+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arsenic
the presence of Cd2+, As3+ or As5+ is required for activity
As3+
70fold activation at 0.05 mM, recombinant MBP-tagged isozyme PCS1
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
Cd2+
the activity of PCS requires Cd and is enhanced by protein phosphorylation
Cd2+
K9S8X3
in presence of 0.1 mM Cd2+, enzyme produces in vitro PC2, and also detectable levels of PC3 and PC4. Catalytic activity increases by 91%. In the absence of Cd2+, only PC2 is produced
Cd2+
the presence of Cd2+, As3+ or As5+ is required for activity
Cd2+
in presence of 0.1 mM Cd2+, enzyme produces in vitro PC2, and also detectable levels of PC3 and PC4. Catalytic activity increases by 77%
Cd2+
50fold activation at 0.05 mM, recombinant MBP-tagged isozyme PCS1
additional information
OsPCS1 is more sensitive to activation by As than by cadmium, whereas OsPCS2 is more weakly activated by As than by cadmium
-
additional information
OsPCS1 is more sensitive to activation by As than by cadmium, whereas OsPCS2 is more weakly activated by As than by cadmium
-
additional information
isozyme OsPCS1 is more strongly activated by As3+ than by Cd2+, and it is vice versa for expression of OsPCS2
-
additional information
isozyme OsPCS1 is more strongly activated by As3+ than by Cd2+, and it is vice versa for expression of OsPCS2
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
Cd2+-bis-glutathionate
in the presence of 0.02 mM GSH, at pH 8.0, temperature not specified in the publication
0.0025
Cd2+-bis-glutathionate
in the presence of 0.04 mM GSH, at pH 8.0, temperature not specified in the publication
0.0016
Zn2+-bis-glutathionate
in the presence of 0.02 mM GSH, at pH 8.0, temperature not specified in the publication
0.0018
Zn2+-bis-glutathionate
in the presence of 0.04 mM GSH, at pH 8.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.8
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected from water samples taken in 2010 at the CEM station of Rio Tinto (SW Spain)
-
-
brenda
collected from water samples taken in 2010 at the RICHI sampling station of Rio Tinto (SW Spain)
-
-
brenda
collected from water samples taken in 2010 at the RICHI sampling station of Rio Tinto (SW Spain)
-
-
brenda
collected from freshwater springs located in Parma surroundings (Italy) in April-May 2014/15/16
-
-
brenda
has a second gene (AtPCS2) encoding another functional phytochelatin synthase
-
-
brenda
collected from water samples taken in 2010 at the CEM station of Rio Tinto (SW Spain)
-
-
brenda
SAG 25.82, UTEX 2576, i.e. Anabaena sp. PCC 7120
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
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
brenda
isoform PCS1 expression levels are higher in roots than in leaves and stems
brenda
isoform PCS1 has a very low basal expression level in untreated whole seedlings
brenda
additional information
expression pattern of isozymes AdPCS1-3 in different organs/tissues of Arundo donax, semi-quantitative RT-PCR expression analysis, overview
brenda
additional information
expression pattern of isozymes AdPCS1-3 in different organs/tissues of Arundo donax, semi-quantitative RT-PCR expression analysis, overview
brenda
additional information
expression pattern of isozymes AdPCS1-3 in different organs/tissues of Arundo donax, semi-quantitative RT-PCR expression analysis, overview
brenda
additional information
-
expression pattern of isozymes AdPCS1-3 in different organs/tissues of Arundo donax, semi-quantitative RT-PCR expression analysis, overview
brenda
additional information
-
the cells are grown in the presence of the antibiotics vancomycin, cefotaxime, and chloramphenicol
brenda
additional information
-
the cells are grown in the presence of the antibiotics vancomycin, cefotaxime, and chloramphenicol
-
brenda
additional information
root- and shoot-specific differential ratios of alternatively spliced OsPCS2a and OsPCS2b transcript expressions are observed under cadmium stress. OsPCS1 is synthesized in roots, shoots and developing seeds
brenda
additional information
root- and shoot-specific differential ratios of alternatively spliced OsPCS2a and OsPCS2b transcript expressions are observed under cadmium stress. OsPCS1 is synthesized in roots, shoots and developing seeds
brenda
additional information
-
root- and shoot-specific differential ratios of alternatively spliced OsPCS2a and OsPCS2b transcript expressions are observed under cadmium stress. OsPCS1 is synthesized in roots, shoots and developing seeds
brenda
additional information
root- and shoot-specific differential ratios of alternatively spliced OsPCS2a and OsPCS2b transcript expressions are observed under cadmium stress. OsPCS2a and OsPCS2b are synthesized in roots, shoots and developing seeds, albeit at different level
brenda
additional information
root- and shoot-specific differential ratios of alternatively spliced OsPCS2a and OsPCS2b transcript expressions are observed under cadmium stress. OsPCS2a and OsPCS2b are synthesized in roots, shoots and developing seeds, albeit at different level
brenda
additional information
-
root- and shoot-specific differential ratios of alternatively spliced OsPCS2a and OsPCS2b transcript expressions are observed under cadmium stress. OsPCS2a and OsPCS2b are synthesized in roots, shoots and developing seeds, albeit at different level
brenda
additional information
-
root- and shoot-specific differential ratios of alternatively spliced OsPCS2a and OsPCS2b transcript expressions are observed under cadmium stress. OsPCS1 is synthesized in roots, shoots and developing seeds
-
brenda
additional information
-
root- and shoot-specific differential ratios of alternatively spliced OsPCS2a and OsPCS2b transcript expressions are observed under cadmium stress. OsPCS2a and OsPCS2b are synthesized in roots, shoots and developing seeds, albeit at different level
-
brenda
additional information
the expression level of isozyyme OsPCS2 is higher than that of isozyme OsPCS1 in the shoots and roots of rice plants. The expression pattern of OsPCS1 splice variants is not changed by Cd or As stress in both shoots and roots
brenda
additional information
the expression level of isozyyme OsPCS2 is higher than that of isozyme OsPCS1 in the shoots and roots of rice plants. The expression pattern of OsPCS1 splice variants is not changed by Cd or As stress in both shoots and roots
brenda
additional information
the expression level of isozyyme OsPCS2 is higher than that of isozyme OsPCS1 in the shoots and roots of rice plants
brenda
additional information
the expression level of isozyyme OsPCS2 is higher than that of isozyme OsPCS1 in the shoots and roots of rice plants
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
contrasting effects of enzyme mutation on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
physiological function
additional information
evolution
-
genes encoding phytochelatin synthases have been found in all vascular plants as well as some algae, fungi, diatoms and invertebrates. Horizontal gene transfer of phytochelatin synthases from bacteria to extremophilic green algae. A detailed phylogenetic analysis gives insight into the complicated evolutionary history of PCS genes and provides evidence for multiple horizontal gene transfer events from bacteria to eukaryotes within the gene family. A separate subgroup containing PCS-like genes within the PCS gene family is not supported since the PCS genes are monophyletic only when the PCS-like genes are included. Genotyping, overview
evolution
the two CDSs of OsPCS1 and OsPCS2 show 72% sequence identity at the nucleotide level, whereas the two proteins share overall 62.1% amino acid sequence identity. Moreover, both the intron sizes and nucleotide sequences are found to be highly differing between OsPCS1 and OsPCS2. Alignment of the deduced OsPCS1 and OsPCS2 polypeptides indicate the presence of N-terminal Phytochelatin (pfam05023) domain with high sequence identity (80.7%) including the conserved catalytic triad of Cys (C), His (H) and Asp (D). On the other hand, the C-terminal Phytochelatin_C (pfam09328) domain show moderate identity (57.68%) between these two polypeptides
evolution
evolution and functional differentiation of the recently diverged three phytochelatin synthase genes from Arundo donax, phylogenetic analysis and evolutionary modeling, overview. AdPCS1-3 proteins are significantly less divergent than other duplicated PCSs, displaying only 25-29 substitutions. All the canonical features of PCSs are present, namely the catalytic triad Cys56, His162, and Asp180. The lengths of both N- and C-terminal domains are comparable to those of previously validated PCSs. AdPCS1-3 genes evolved at different evolutionary rates
evolution
-
genes encoding phytochelatin synthases have been found in all vascular plants as well as some algae, fungi, diatoms and invertebrates. Horizontal gene transfer of phytochelatin synthases from bacteria to extremophilic green algae. A detailed phylogenetic analysis gives insight into the complicated evolutionary history of PCS genes and provides evidence for multiple horizontal gene transfer events from bacteria to eukaryotes within the gene family. A separate subgroup containing PCS-like genes within the PCS gene family is not supported since the PCS genes are monophyletic only when the PCS-like genes are included. Genotyping, overview
evolution
-
the two CDSs of OsPCS1 and OsPCS2 show 72% sequence identity at the nucleotide level, whereas the two proteins share overall 62.1% amino acid sequence identity. Moreover, both the intron sizes and nucleotide sequences are found to be highly differing between OsPCS1 and OsPCS2. Alignment of the deduced OsPCS1 and OsPCS2 polypeptides indicate the presence of N-terminal Phytochelatin (pfam05023) domain with high sequence identity (80.7%) including the conserved catalytic triad of Cys (C), His (H) and Asp (D). On the other hand, the C-terminal Phytochelatin_C (pfam09328) domain show moderate identity (57.68%) between these two polypeptides
-
evolution
-
genes encoding phytochelatin synthases have been found in all vascular plants as well as some algae, fungi, diatoms and invertebrates. Horizontal gene transfer of phytochelatin synthases from bacteria to extremophilic green algae. A detailed phylogenetic analysis gives insight into the complicated evolutionary history of PCS genes and provides evidence for multiple horizontal gene transfer events from bacteria to eukaryotes within the gene family. A separate subgroup containing PCS-like genes within the PCS gene family is not supported since the PCS genes are monophyletic only when the PCS-like genes are included. Genotyping, overview
-
evolution
-
genes encoding phytochelatin synthases have been found in all vascular plants as well as some algae, fungi, diatoms and invertebrates. Horizontal gene transfer of phytochelatin synthases from bacteria to extremophilic green algae. A detailed phylogenetic analysis gives insight into the complicated evolutionary history of PCS genes and provides evidence for multiple horizontal gene transfer events from bacteria to eukaryotes within the gene family. A separate subgroup containing PCS-like genes within the PCS gene family is not supported since the PCS genes are monophyletic only when the PCS-like genes are included. Genotyping, overview
-
malfunction
the As(III)-sensitive phenotype of cad1-3 seedlings is completely rescued by the introduction of OsPCS1full variant, whereas growth of the plants expressing the other OsPCS1 variants is inhibited by As(III) as strongly as that of cad1-3. Similarly, OsPCS1full introduction complements the Cd-sensitive phenotype of cad1-3, while the other OsPCS1 variants do not. OsPCS1 mutant plants show increased sensitivity to Cd and As(III) stress. Distribution of As and Cd is altered in shoot and grains of OsPCS1 mutants
malfunction
the As(III)-sensitive phenotype of cad1-3 seedlings is completely rescued by the introduction of OsPCS1full variant, whereas growth of the plants expressing the other OsPCS1 variants is inhibited by As(III) as strongly as that of cad1-3. Similarly, OsPCS1full introduction complements the Cd-sensitive phenotype of cad1-3, while the other OsPCS1 variants do not
malfunction
the As(III)-sensitive phenotype of cad1-3 seedlings is completely rescued by the introduction of OsPCS1full variant, whereas growth of the plants expressing the other OsPCS1 variants is inhibited by As(III) as strongly as that of cad1-3. Similarly, OsPCS1full introduction complements the Cd-sensitive phenotype of cad1-3, while the other OsPCS1 variants do not. OsPCS1 mutant plants show increased sensitivity to Cd and As(III) stress
malfunction
the As(III)-sensitive phenotype of cad1-3 seedlings is completely rescued by the introduction of OsPCS1full variant, whereas growth of the plants expressing the other OsPCS variants is inhibited by As(III) as strongly as that of cad1-3. Similarly, OsPCS1full introduction complements the Cd-sensitive phenotype of cad1-3, while the other OsPCS1 variants do not. OsPCS1 mutant plants show increased sensitivity to Cd and As(III) stress
malfunction
transgenic plants highly expressing OsPCS1 show significantly lower As levels in grains than do wild-type plants
malfunction
RNAi-mediated grain-specific silencing of OsPCS decreases cadmium accumulation in rice grain
malfunction
genetically engineered plants having their OsPCS1 expression silenced via RNA interference (OsPCS1 RNAi) show no significant difference phenotype compared to wild-type plants. Treatment with buthionine sulfoximine, an inhibitor of GSH biosynthesis, significantly decreases Cd and As tolerance of rice seedlings. Concentrations of thiol peptides in the roots of OsPCS RNAi plants grown under Cd stress, overview
malfunction
genetically engineered plants having their OsPCS2 expression silenced via RNA interference (OsPCS2 RNAi) contain less phytochelatins (PCs) and more glutathione (GSH), the substrate of PC synthesis by PCS, than wild-type plants. OsPCS2 RNAi plants are sensitive to As(III) stress, but Cd tolerance is little affected. Treatment with buthionine sulfoximine, an inhibitor of GSH biosynthesis, significantly decreases Cd and As tolerance of rice seedlings. Concentrations of thiol peptides in the roots of OsPCS RNAi plants grown under Cd stress, overview
malfunction
AtPCS2-overexpressing transgenic Arabidopsis thaliana and Nicotiana tabacum plants display increased seed germination rates and seedling growth under high salt stress. In addition, transgenic Arabidopsis subjected to salt stress exhibit enhanced proline accumulation and reduced Na+/K+ ratios compared to wild-type plants. Effects of salt stress on seed germination and root elongation of AtPCS2-overexpressing transgenic plants, phenotype, overview
malfunction
-
AtPCS2-overexpressing transgenic Arabidopsis thaliana and Nicotiana tabacum plants display increased seed germination rates and seedling growth under high salt stress. In addition, transgenic Arabidopsis subjected to salt stress exhibit enhanced proline accumulation and reduced Na+/K+ ratios compared to wild-type plants. Effects of salt stress on seed germination and root elongation of AtPCS2-overexpressing transgenic plants, phenotype, overview
-
malfunction
-
RNAi-mediated grain-specific silencing of OsPCS decreases cadmium accumulation in rice grain
-
physiological function
phytochelatins play an important role in detoxification of heavy metals in plants
physiological function
the enzyme is involved in cellular cadmium tolerance
physiological function
the enzyme is involved in cellular cadmium tolerance
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
enhanced metal (Cd2+ and As5+) accumulation is due to post-translational activation of the enzyme in the presence of Cd2+ ion
physiological function
the enzyme binds, localizes, stores or sequesters heavy metals in plant cells
physiological function
-
the enzyme has a major role in the detoxification of heavy metals. Escherichia coli with overexpressed phytochelatin synthase 1 has enhanced tolerance to cadmium, copper, sodium, and mercury
physiological function
the enzyme confers resistance on Cd2+ stress
physiological function
-
phytochelatins (PCs) mediate high-affinity binding and contribute to detoxification of heavy metal ions and metalloids, such as cadmium or arsenic, by promoting the vacuolysosomal sequestration of heavy metals. These compounds are enzymatically synthesized from reduced glutathione (GSH) and related thiols in a gamma-glutamylcysteinyltranspeptidation reaction catalyzed by phytochelatin synthase (PCS)
physiological function
phytochelatin synthase has contrasting effects on cadmium and arsenic accumulation in rice grains. Physiological role of Oryza sativa phytochelatin synthase 1full (OsPCS1full) in the distribution and detoxification of arsenic (As) and cadmium (Cd), importance of OsPCS1-dependent PC synthesis for rice As(III) and Cd tolerance
physiological function
phytochelatin synthase has contrasting effects on cadmium and arsenic accumulation in rice grains
physiological function
phytochelatin synthase has contrasting effects on cadmium and arsenic accumulation in rice grains. Physiological role of Oryza sativa phytochelatin synthase 1 (OsPCS1) in the distribution and detoxification of arsenic (As) and cadmium (Cd), importance of OsPCS1-dependent PC synthesis for rice As(III) and Cd tolerance
physiological function
phytochelatin synthase OsPCS1 plays a crucial role in reducing arsenic levels in rice grains. Redundancy between OsPCS1 and OsPCS2
physiological function
redundancy between OsPCS1 and OsPCS2
physiological function
-
in plant cells, Cd ions are highly noxious even at low concentrations, with subsequent severe negative effects. Activation of phytochelatin synthase (PCS) and glutathione-S-transferase, but minimally phytochelatin synthesis, play a role to counteract Cd toxicity in Leptodictyum riparium, for minimizing the cellular damage caused by the metal. The highest Cd concentrations activates the formation of gamma-glutamyl-cysteinyl-bimane (GS-bimane) in the cytosol, possibly catalyzed by the peptidase activity of phytochelatin synthase. PCS activation is self-regulated, because its product poly(4-glutamyl-cysteinyl)glycine (PCn) chelates Cd, and the reaction stops when free Cd2+ ions are no longer available. Besides being a gamma-EC transpeptidase, PCS is also a cysteine peptidase that may regulate the cytosolic catabolism of gamma-glutamyl-cysteinyl (GS)-conjugates. In this case, GS-conjugates with MCB (GS-bimane) can be cleaved into gamma-gamma-glutamyl-cysteine and glycine, a reaction stimulated by some metals, particularly Cd, Zn, and Cu
physiological function
the OsPCS2 exhibits root- and shoot-specific differential ratios of alternatively spliced transcripts in Oryza sativa subsp. indica rice under Cd stress, and plays role in Cd and As stress tolerance and accumulation
physiological function
-
analysis of the possible involvement of the enzyme in the homeostasis of metallic micronutrients, and its role in the detoxification of non-essential metals, such as Cd2+. Neither in vivo nor in vitro exposure to Zn results in PCS activation and significant phytochelatin (PC) biosynthesis, while Fe(II)/(III) and Cd2+ are able to activate enzyme PCS in vitro, as well as to induce PC accumulation in vivo. Function of enzyme PCS and phytochelatins in managing Fe homeostasis in the carophyte Nitella mucronata
physiological function
role of of enzyme PCS in abiotic stress tolerance
physiological function
pyhtochelatins (PCs) are important for As tolerance in rice. PC synthesis may make a smaller contribution to Cd tolerance in rice. Synthesis of thiol peptides in response to Cd or As(III) stress in rice roots
physiological function
isozyme OsPCS2 is a major isozyme controlling phytochelatin (PC) synthesis, and PCs are important for As tolerance in rice. PC synthesis may make a smaller contribution to Cd tolerance in rice. Synthesis of thiol peptides in response to Cd or As(III) stress in rice roots
physiological function
phytochelatin synthase (PCS) is an enzyme that synthesizes phytochelatins, which are metal-binding peptides. It plays an important role in heavy metal detoxification or tolerance. Function of Arabidopsis thaliana phytochelatin synthase 2 (AtPCS2) in the salt stress response. AtPCS2 plays a positive role in seed germination and seedling growth under salt stress through a series of indirect effects that are likely involved in H2O2 scavenging, regulation of osmotic adjustment and ion homeostasis
physiological function
phytochelatin synthase (PCS) is an enzyme involved in the synthesis of phytochelatins, cysteine-rich peptides which play a key role in heavy metal (HM) detoxification of plants. Mulberry has the potential to remediate HM-contaminated soils. The two PCS genes in Morus notabilis (PCS1 and 2) are involved in HM detoxification in Morus. MnPCS1 plays a more important role in Cd detoxification than MnPCS2. MnPCS enzymes can markedly increase the tolerance of the transgenic plants at high concentrations of Zn2+, while the corresponding relationship between Cd2+ accumulation and the expression of MnPCSs are not observed. There might be some factor-dependent posttranscriptional regulation of PCS, like intron-mediated enhancement, and/or an optimum PCS level for tolerance to and accumulation of HMs in plants
physiological function
phytochelatin synthase (PCS) is an enzyme involved in the synthesis of phytochelatins, cysteine-rich peptides which play a key role in heavy metal (HM) detoxification of plants. Mulberry has the potential to remediate HM-contaminated soils. The two PCS genes in Morus notabilis (PCS1 and 2) are involved in HM detoxification in Morus. MnPCS1 plays a more important role in Cd detoxification than MnPCS2. The enzymes can markedly increase the tolerance of the transgenic plants at high concentrations of Zn2+, while the corresponding relationship between Cd2+ accumulation and the expression of MnPCSs are not observed. There might be some factor-dependent posttranscriptional regulation of PCS, like intron-mediated enhancement, and/or an optimum PCS level for tolerance to and accumulation of HMs in plants
physiological function
phytochelatin synthases (PCSs) play pivotal roles in the detoxification of heavy metals and metalloids in plants
physiological function
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phytochelatins (PCs) mediate high-affinity binding and contribute to detoxification of heavy metal ions and metalloids, such as cadmium or arsenic, by promoting the vacuo-lysosomal sequestration of heavy metals. These compounds are enzymatically synthesized from reduced glutathione (GSH) and related thiols in a gamma-glutamylcysteinyltranspeptidation reaction catalyzed by phytochelatin synthase (PCS)
physiological function
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PCS1 overexpression or cooverexpression with glutamate-cysteine ligase GSH1 significantly improves Cd tolerance and accumulation capacity in yeast. PCS1 overexpression in Spirodela polyrhiza promotes Cd, Fe, Mn, and Ca accumulation and might promote GSH and phytochelatins synthesis
physiological function
Nicotiana tabacum lines overexpressing PCS1 produced more phytochelatins than wild-type plants when grown under CdCl2 stress. This does not result in increased Cd accumulation but increases sensitivity to Cd. The application of exogenous GSH leads to a enhanced Cd accumulation in the PCS1overexpressing lines. Heterologous expression of PCS1 results in enhanced Cd tolerance in an Arabidopsis thaliana PCS1 mutant
physiological function
expression of a truncated PCS1 lacking a C-terminal 149-amino acid fragment in yeast complements the Cd-sensitive phenotype of the ycf1DELTA mutant strain, improves the Cd tolerance of the wild-type and promotes Cd accumulation in the yeast cells. Overexpression of truncated PCS1 in Arabidopsis thaliana improves the Cd tolerance slightly, has little impact on Cd accumulation in transgenic plants
physiological function
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expression of isoform PCS1 in yeast cells lacking cadmium factor (YCF1) confers resistance to Cd, Pb and Zn
physiological function
overexpression lines of PCS1 exhibit better root growth and fresh weight, lower level of lipid peroxidation product MDA and H2O2, and higher Cd accumulation and translocation factor compared to the wild-type under Cd stress
physiological function
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heterologous expression of PCS2 in Escherichia coli leads to increased tolerance to exposure to Ni, Co, Cu and arsenic (As), as well as to acidic pH and exposure to UVB, salt, or perchlorate
physiological function
silencing of PCS leads to blockage of phytochelatin synthesis and severely inhibits plant growth by promoting the excess accumulation of H2O2 and MDA. Melatonin pretreatment regulates nutrient homeostasis to combat the stress generated by the presence of Cd. Silencing of the PCS gene largely abolishes the mitigation effects of melatonin
physiological function
in presence of Cd2+, PCS1 mutant strains contain higher amounts of GS-bimane and lower amounts of gamma-Glu-Cys-bimane compared to wild-type
physiological function
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phytochelatin synthase (PCS) is an enzyme that synthesizes phytochelatins, which are metal-binding peptides. It plays an important role in heavy metal detoxification or tolerance. Function of Arabidopsis thaliana phytochelatin synthase 2 (AtPCS2) in the salt stress response. AtPCS2 plays a positive role in seed germination and seedling growth under salt stress through a series of indirect effects that are likely involved in H2O2 scavenging, regulation of osmotic adjustment and ion homeostasis
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physiological function
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the OsPCS2 exhibits root- and shoot-specific differential ratios of alternatively spliced transcripts in Oryza sativa subsp. indica rice under Cd stress, and plays role in Cd and As stress tolerance and accumulation
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physiological function
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phytochelatins (PCs) mediate high-affinity binding and contribute to detoxification of heavy metal ions and metalloids, such as cadmium or arsenic, by promoting the vacuolysosomal sequestration of heavy metals. These compounds are enzymatically synthesized from reduced glutathione (GSH) and related thiols in a gamma-glutamylcysteinyltranspeptidation reaction catalyzed by phytochelatin synthase (PCS)
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physiological function
-
phytochelatins (PCs) mediate high-affinity binding and contribute to detoxification of heavy metal ions and metalloids, such as cadmium or arsenic, by promoting the vacuo-lysosomal sequestration of heavy metals. These compounds are enzymatically synthesized from reduced glutathione (GSH) and related thiols in a gamma-glutamylcysteinyltranspeptidation reaction catalyzed by phytochelatin synthase (PCS)
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additional information
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the cosmopolitan moss Leptodictyum riparium (Bryophyta) can accumulate, and seemingly tolerate, very high concentrations of toxic metals, including Cd. Leptodictyum riparium performs little Cd immobilization at the cell wall level, and therefore the metal enters the cytosol rather easily
additional information
a conserved N-terminus contains the catalytic triad Cys58, His164, Asp182, and a flexible C-terminal region contains a C371C372QETC376VKC379 motif
Show AA Sequence and Transmembrane Helices (2782 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
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
54000
55000
56000
56300
56500
56300
AtPCS1, residues 1-485, theoretical, verified by SDS-PAGE and Western Blot analysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the OsPCS1full variant shows an AtPCS1/2-like structure with two domains
additional information
the OsPCS1full variant shows an AtPCS1/2-like structure with two domains
additional information
the OsPCS1full variant shows an AtPCS1/2-like structure with two domains
additional information
the OsPCS1full variant shows an AtPCS1/2-like structure with two domains
additional information
the OsPCS1full variant shows an AtPCS1/2-like structure with two domains
additional information
the OsPCS2 structure lacks the C-terminal domain
additional information
the OsPCS2 structure lacks the C-terminal domain
additional information
the OsPCS2 structure lacks the C-terminal domain
additional information
the OsPCS2 structure lacks the C-terminal domain
additional information
the OsPCS2 structure lacks the C-terminal domain
additional information
the OsPCS1a variant consists of only the N-terminal domain
additional information
the OsPCS1a variant consists of only the N-terminal domain
additional information
the OsPCS1a variant consists of only the N-terminal domain
additional information
the OsPCS1a variant consists of only the N-terminal domain
additional information
the OsPCS1a variant consists of only the N-terminal domain
additional information
the OsPCS1b variant consists of only the C-terminal domain
additional information
the OsPCS1b variant consists of only the C-terminal domain
additional information
the OsPCS1b variant consists of only the C-terminal domain
additional information
the OsPCS1b variant consists of only the C-terminal domain
additional information
the OsPCS1b variant consists of only the C-terminal domain
additional information
the OsPCS1c variant consists only of a very short fragment of the catalytic N-terminal domain
additional information
the OsPCS1c variant consists only of a very short fragment of the catalytic N-terminal domain
additional information
the OsPCS1c variant consists only of a very short fragment of the catalytic N-terminal domain
additional information
the OsPCS1c variant consists only of a very short fragment of the catalytic N-terminal domain
additional information
the OsPCS1c variant consists only of a very short fragment of the catalytic N-terminal domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
PCS1 expressed in Escherichia coli is phosphorylated at a Thr residue near its catalytic site
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C109S
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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
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C113S
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C56S
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mutation abolishes Cd2+ tolerance observed with wild-type enzyme, causes negligible intracellular phytochelatin accumulation
C90A
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C90S
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C91A
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C91S
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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
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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
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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
T49A
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
additional information
T49A
AtPCS1 mutant, Thr49 is the only residue to be phosphorylated
T49A
AtPCS1-N mutant, Thr49 is the only residue to be phosphorylated
additional information
AtPCS2-overexpressing transgenic Arabidopsis thaliana and Nicotiana tabacum plants display increased seed germination rates and seedling growth under high salt stress. Furthermore, decreased levels of hydrogen peroxide (H2O2) and lipid peroxidation are observed in transgenic Arabidopsis thaliana compared to wild-type specimens. Salt stress greatly reduces transcript levels of CuSOD2, FeSOD2, CAT2, and GR2 in wild-type but not in transgenic Arabidopsis thaliana. Levels of CAT3 in transgenic Arabidopsis are markedly increased upon salt stress, suggesting that low accumulation of H2O2 in transgenic Arabidopsis is partially achieved through induction of CAT
additional information
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AtPCS2-overexpressing transgenic Arabidopsis thaliana and Nicotiana tabacum plants display increased seed germination rates and seedling growth under high salt stress. Furthermore, decreased levels of hydrogen peroxide (H2O2) and lipid peroxidation are observed in transgenic Arabidopsis thaliana compared to wild-type specimens. Salt stress greatly reduces transcript levels of CuSOD2, FeSOD2, CAT2, and GR2 in wild-type but not in transgenic Arabidopsis thaliana. Levels of CAT3 in transgenic Arabidopsis are markedly increased upon salt stress, suggesting that low accumulation of H2O2 in transgenic Arabidopsis is partially achieved through induction of CAT
additional information
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AtPCS2-overexpressing transgenic Arabidopsis thaliana and Nicotiana tabacum plants display increased seed germination rates and seedling growth under high salt stress. Furthermore, decreased levels of hydrogen peroxide (H2O2) and lipid peroxidation are observed in transgenic Arabidopsis thaliana compared to wild-type specimens. Salt stress greatly reduces transcript levels of CuSOD2, FeSOD2, CAT2, and GR2 in wild-type but not in transgenic Arabidopsis thaliana. Levels of CAT3 in transgenic Arabidopsis are markedly increased upon salt stress, suggesting that low accumulation of H2O2 in transgenic Arabidopsis is partially achieved through induction of CAT
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additional information
the lack of a C-terminal 149-amino acid fragment does not affect its Cd tolerance, but might restrict the zinc (Zn) detoxification in yeast
additional information
Zn2+/Cd2+ concentrations in both shoots and roots of the transgenic Arabidopsis seedlings expressing PCS1 and/or PCS2 are higher than in wild-type seedlings at two different Zn2+/Cd2+ concentrations. In addition, there is a positive correlation between Zn2+ accumulation and the expression level of MnPCS1 or MnPCS2
additional information
Zn2+/Cd2+ concentrations in both shoots and roots of the transgenic Arabidopsis seedlings expressing PCS1 and/or PCS2 are higher than in wild-type seedlings at two different Zn2+/Cd2+ concentrations. In addition, there is a positive correlation between Zn2+ accumulation and the expression level of MnPCS1 or MnPCS2
additional information
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Zn2+/Cd2+ concentrations in both shoots and roots of the transgenic Arabidopsis seedlings expressing PCS1 and/or PCS2 are higher than in wild-type seedlings at two different Zn2+/Cd2+ concentrations. In addition, there is a positive correlation between Zn2+ accumulation and the expression level of MnPCS1 or MnPCS2
additional information
an extra copy of phytochelatin-encoding gene phytochelatin synthase (pcs) is constitutively expressed in Anabaena sp. strain PCC7120 (An7120), an integrative expression vector pFPN is used for incorporating a cassette of genes for genomic integration and expression. Comparative growth behavior of wild-type strain and overexpressed strain AnFPN-pcs under LC50 doses of UV-B, salt, heat, copper, carbofuran, and cadmium resulted in decrement in specific growth rate by 26, 21, 27, 13, 30, and 17%, respectively, in An7120 compared to AnFPN-pcs thereby suggesting that the transformed cyanobacterium AnFPN-pcs has developed tolerance and hence shows better growth performances under different abiotic stresses. Comparison of differentially expressed proteins in An7120 and AnFPN-pcs, and dynamics of differentially expressed proteins in An7120 and AnFPN-pcs, overview
additional information
analysis of the transgenic rice lines grown under metal(loid) stress revealed almost complete absence of both OsPCS1 and OsPCS2 transcripts in the developing seeds couples with the significant reduction in the content of Cd (about 51%) and As (about 35%) in grains compared with the non-transgenic plant. Taken together, the findings indicate towards a crucial role played by the tissue-specific alternative splicing and relative abundance of the OsPCS2 gene during heavy metal(loid) stress mitigation in rice plant
additional information
analysis of the transgenic rice lines grown under metal(loid) stress revealed almost complete absence of both OsPCS1 and OsPCS2 transcripts in the developing seeds couples with the significant reduction in the content of Cd (about 51%) and As (about 35%) in grains compared with the non-transgenic plant. Taken together, the findings indicate towards a crucial role played by the tissue-specific alternative splicing and relative abundance of the OsPCS2 gene during heavy metal(loid) stress mitigation in rice plant
additional information
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analysis of the transgenic rice lines grown under metal(loid) stress revealed almost complete absence of both OsPCS1 and OsPCS2 transcripts in the developing seeds couples with the significant reduction in the content of Cd (about 51%) and As (about 35%) in grains compared with the non-transgenic plant. Taken together, the findings indicate towards a crucial role played by the tissue-specific alternative splicing and relative abundance of the OsPCS2 gene during heavy metal(loid) stress mitigation in rice plant
additional information
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analysis of the transgenic rice lines grown under metal(loid) stress revealed almost complete absence of both OsPCS1 and OsPCS2 transcripts in the developing seeds couples with the significant reduction in the content of Cd (about 51%) and As (about 35%) in grains compared with the non-transgenic plant. Taken together, the findings indicate towards a crucial role played by the tissue-specific alternative splicing and relative abundance of the OsPCS2 gene during heavy metal(loid) stress mitigation in rice plant
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additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. Thee mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. Thee mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. Thee mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. Thee mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. Thee mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. The mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. The mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. The mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. The mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. The mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
isolation of two rice mutants (has1 and has2) in which As levels are much higher in grains but significantly lower in node I compared with the wild-type. Map-based cloning identifies the genes responsible as OsABCC1 in has1 and OsPCS1 in has2. F2 progeny obtained by crossing the mutant lines with the indica rice cultivar Habataki are genotyped by using polymorphism between cvs. Koshihikari and Habataki and measurements of As levels in grains from the F2 plants. The frequency of the high-As phenotype in F2 progeny is below 50%, suggesting that has1 and has2 are recessive mutants. Genetic linkage analyses indicate that the high-As mutant phenotypes are tightly linked to single regions on chromosome 4 in has1 and on chromosome 5 in has2
additional information
isolation of two rice mutants (has1 and has2) in which As levels are much higher in grains but significantly lower in node I compared with the wild-type. Map-based cloning identifies the genes responsible as OsABCC1 in has1 and OsPCS1 in has2. F2 progeny obtained by crossing the mutant lines with the indica rice cultivar Habataki are genotyped by using polymorphism between cvs. Koshihikari and Habataki and measurements of As levels in grains from the F2 plants. The frequency of the high-As phenotype in F2 progeny is below 50%, suggesting that has1 and has2 are recessive mutants. Genetic linkage analyses indicate that the high-As mutant phenotypes are tightly linked to single regions on chromosome 4 in has1 and on chromosome 5 in has2
additional information
silencing of OsPCS1 expression via RNA interference by OsPCS1 RNAi introduced into rice via Agrobacterium tumefaciens strain EHA105 transfection method. Phenotypes, overview
additional information
silencing of OsPCS1 expression via RNA interference by OsPCS1 RNAi introduced into rice via Agrobacterium tumefaciens strain EHA105 transfection method. Phenotypes, overview
additional information
silencing of OsPCS2 expression via RNA interference by OsPCS2 RNAi introduced into rice via Agrobacterium tumefaciens strain EHA105 transfection method. Phenotypes, overview
additional information
silencing of OsPCS2 expression via RNA interference by OsPCS2 RNAi introduced into rice via Agrobacterium tumefaciens strain EHA105 transfection method. Phenotypes, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM Tris-HCl, pH 8.0, 1 mM mercaptoethanol, 20% glycerol and 1% bovine serum albumin
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Toyopearl column chromatography, HiTrap SP column chromatography, and Hitrap Q sepharose column chromatography
Ni2+ affinity column chromatography and HisTrap HP column chromatography
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recombinant enzyme
Talon metal affinity resin column chromatography, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtPCS2-gene expressed in Schizosaccharomyces pombe strain FY254, a phytochelatin synthase knockout strain
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expressed in a Arabidopsis thaliana cad1-3 phytochelatin-deficient mutant and in Nicotiana tabacum cultivar Petit Havana
expressed in Arabidopsis thaliana via transformation with Agrobacterium tumefaciens strain EHA105
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells and Saccharomyces cerevisiae strain TY167
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae strain BY4741
expressed in Saccharomyces cerevisiae strain YK44 and Nicotiana tabacum strain NC89
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expressed in Schizosaccharomyces pombe strain SP27, a phytochelatin synthase knockout strain
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expression in Escherichia coli and Saccharomyces cerevisiae to enhance tolerance to toxicity of cadmium ion
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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
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expression in Saccharomyces cerevisiae. Yeast cells expressing LjPCS3 show increased in vivo tolerance to Cd
expression of GST-PCS in Echerichia coli is the optimum method for expression of this enzyme
fused to a C-terminal Flag epitope
gene alr0975 or pcs, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain DH5alpha, and functional constitutive overexpression in Anabaena sp. strain PCC 7120, semiquantitative RT-PCR enzyme expression analysis
gene CaPCS1, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotyping, recombinant expression in Escherichia coli improves the cadmium resistance of the bacteria, quantitative RT-PCR enzyme expression analysis
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gene CaPCS2, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotyping, recombinant expression in Escherichia coli improves the cadmium resistance of the bacteria, quantitative RT-PCR enzyme expression analysis
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gene DaPCS1, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotyping, recombinant expression in Escherichia coli, quantitative RT-PCR enzyme expression analysis
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gene OsPCS1, recombinant expression in Escherichia coli, recombinant expression of MBP-tagged OsPCS1 in the has2 mutant under the control of the cauliflower mosaic virus (CaMV) 35S promoter, the nodes of the OsPCS1-overexpressing line show higher As levels than those of the wild-type
gene OsPCS2, recombinant expression in Escherichia coli, recombinant expression of MBP-tagged OsPCS1 in the has2 mutant under the control of the cauliflower mosaic virus (CaMV) 35S promoter. Overexpression of OsPCS2 does not fully complement the has2 mutation, although the As levels in grains became lower than in the non-transgenic has2 mutant
gene PCS1, DNA and amino acid sequence determination and analysis, sequence comparisons, different PCS1 splicing variants are detected, quantitative expression analysis, recombinant expression of MBP-tagged isozyme PCS1
gene PCS1, isolation of four different transcript variants of OsPCS1, and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis revealing that expression of the longest OsPCS1 variant, OsPCS1full, is most abundant, functional recombinant in expression in PCS-deficient
gene PCS1, isolation of four different transcript variants of OsPCS1, and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis revealing that expression of the longest OsPCS1 variant, OsPCS1full, is most abundant, functional recombinant in expression in PCS-deficient mutants of Schizosaccharomyces pombe PCS knockout strain DELTApcs and Arabidopsis thaliana null mutant cad1-3 plants with OsPCS1full possessing good PCS activity in response to As(III) and Cd while the activity of the other PCS variants is very low
gene PCS1, isolation of four different transcript variants of OsPCS1, and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis revealing that expression of the longest OsPCS1 variant, OsPCS1full, is most abundant, functional recombinant in expression in PCS-deficient mutants of Schizosaccharomyces pombe PCS knockout strain DELTApcs and Arabidopsis thaliana null mutant cad1-3 plants with OsPCS1full possessing good PCS activity in response to As(III) and Cd while the activity of the other PCS variants is very low. Transcript of the introduced OsPCS genes is evident in all cad1-3/OsPCS lines except for cad1-3/OsPCS1b line
gene PCS1, isolation of four different transcript variants of OsPCS1, DNA and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis revealing that expression of the longest OsPCS1 variant, OsPCS1full, is most abundant, functional recombinant in expression in PCS-deficient mutants of Schizosaccharomyces pombe PCS knockout strain DELTApcs and Arabidopsis thaliana null mutant cad1-3 plants with OsPCS1full possessing good PCS activity in response to As(III) and Cd while the activity of the other PCS variants is very low. Phenotypes, overview
gene PCS1, recombinant expression in Escherichia coli strain Rosetta (DE3) pLysS
gene PCS1, sequence comparisons and phylogenetic analysis, recombinant expression in Arabidopsis thaliana Col-0 ecotype, and induction by Cd2+, functional recombinant expression in Saccharomyces cerevisiae YK44 highly Cd2+-sensitive strain conferring Cd resistance. Compared to PCS2 and 3 expressing lines, the AdPCS1 transformant has a longer lag phase, resulting in slower initial growth. This difference is rescued after 24 h, with the growth kinetics of the AdPCS1 transformant becoming normal, indicating that the difference results from decreased translational efficiency
gene PCS1, two Morus notabilis PCS genes are identified based on a genome-wide analysis of the Morus genome database, DNA and amino acid sequence determination and analysis, exon-intron structures of the MnPCS genes, quantitative real-time PCR enzyme expression analysis, expression in Arabidopsis thaliana
gene PCS15, DNA and amino acid sequence determinataion and analysis, RT-PCR expression analysis, recombinant expression in Saccharomyces cerevisiae ycf1 mutant (DELTAycf1) cells (DTY167) confers Cd resistance. The growth of OsPCS15-transformed DELTAycf1 cells is similar to that of empty vector-transformed wild-type and DELTAycf1 cells. Recombinant overexpression of GFP-tagged enzyme PCS15 in Arabidopsis thaliana under control of the CaMV 35S promoter leading to increasing Cd2+ concentrations. Root growth in OsPCS15 transgenic plants is reduced by approximately 26% following treatment with 0.05-0.07 mM CdCl2. In contrast, ectopic expression of PCS15 increases the sensitivity to Cd in Arabidopsis thaliana
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gene PCS2, DNA and amino acid sequence determination and analysis, chromosome 6, genomic organization of OsPCS1 constitutes 5 exons separated by 4 introns, whereas that of OsPCS2 indicates the presence of 6 exons interrupted by 5 introns. Quantitative RT-PCR expression analysis. Among the two PCS genes, OsPCS1 and OsPCS2 in indica rice cultivar, the OsPCS2 produces an alternatively spliced OsPCS2b transcript that bears the unusual premature termination codon besides the canonically spliced OsPCS2a transcript. Root- and shoot-specific differential ratios of alternatively spliced OsPCS2a and OsPCS2b transcript expressions are observed under cadmium stress, recombinant expression in Saccharomyces cerevisiae cells transformed with OsPCS2a exhibits increased cadmium and arsenic tolerance and accumulation, unlike the OsPCS2b transformed yeast cells
gene PCS2, DNA and amino acid sequence determination and analysis, sequence comparisons, different PCS1 splicing variants are detected, quantitative expression analysis, recombinant expression of MBP-tagged isozyme PCS2
gene PCS2, isolation of a single transcript form of OsPCS2, and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis, functional recombinant in expression in PCS-deficient mutants of Schizosaccharomyces pombe PCS knockout strain DELTApcs and Arabidopsis thaliana null mutant cad1-3 plants, the activity of PCS2 in response to As(III) and Cd is very low
gene PCS2, recombinant expression in Arabidopsis thaliana and Nicotiana tabacum var. Xanthi plants using the Agrobacterium tumefaciens strain GV3101 transfection method
gene PCS2, sequence comparisons and phylogenetic analysis, recombinant expression in Arabidopsis thaliana Col-0 ecotype, and induction by Cd2+, functional recombinant expression in Saccharomyces cerevisiae YK44 highly Cd-sensitive strain conferring Cd2+ resistance
gene PCS2, two Morus notabilis PCS genes are identified based on a genome-wide analysis of the Morus genome database, DNA and amino acid sequence determination and analysis, exon-intron structures of the MnPCS genes, quantitative real-time PCR enzyme expression analysis, recombinant expression in Arabidopsis thaliana
gene PCS3, sequence comparisons and phylogenetic analysis, recombinant expression in Arabidopsis thaliana Col-0 ecotype, and induction by Cd2+, functional recombinant expression in Saccharomyces cerevisiae YK44 highly Cd-sensitive strain conferring Cd2+ resistance
gene PCS5, DNA and amino acid sequence determinataion and analysis, RT-PCR expression analysis, recombinant expression in Saccharomyces cerevisiae ycf1 mutant (DELTAycf1) cells (DTY167) confers Cd resistance. The growth of OsPCS5-transformed DELTAycf1 cells is similar to that of empty vector-transformed wild-type and DELTAycf1 cells. Recombinant overexpression of GFP-tagged enzyme PCS5 in Arabidopsis thaliana under control of the CaMV 35S promoter leading to increasing Cd2+ concentrations. Root growth in OsPCS5 transgenic plants is reduced by approximately 33% following treatment with 0.05-0.07 mM CdCl2. In contrast, ectopic expression of PCS5 increases the sensitivity to Cd in Arabidopsis thaliana
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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 pGEM-T easy vector for sequencing, into the vector pYES2 for expression in Saccharomyces cerevisiae cells
into the vector pET-28b for expression in Escherichia coli BL21 Rosetta DE3 pLysS cells
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
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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
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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
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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
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transformed into Saccharomyces cerevisiae DTY167
transformed into Saccharomyces cerevisiae strain DTY67, hypersensitive to Cd2+-stress
G5ECE4
into the binary plasmid vector pCB302 for introducing into Agrobacterium GV3101 strain, tobacco plants are transformed by the standard leaf disc method
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into the binary plasmid vector pCB302 for introducing into Agrobacterium GV3101 strain, tobacco plants are transformed by the standard leaf disc method
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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)
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
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expression of AtPCS2 is significantly decreased in response to high concentrations of metals Ni2+ (0.1 mM), Mg2+ (1.0 mM), Cd2+ (0.3 mM), Hg2+ (0.030 mM), Zn2+ (0.5 mM), and Pb2+ (0.5 mM), as well as by abscisic acid (0.1 mM), PEG (15%) drougth, and cold (4C) stress, overview
expression of AtPCS2 is significantly increased in response to 100 and 200 mM NaCl treatment. In addition, transgenic Arabidopsis subjected to salt stress exhibit enhanced proline accumulation and reduced Na+/K+ ratios compared to wild-type plants. The enzyme expression is also induced by H2O2 at 20 mM
expression of gene AdPCS 1 is responsive to stress through heavy metals
expression of OsPCS1 is upregulated by As(III) stress in the roots
expression of PCS1 is induced in root, stem, and leaf tissues within 24 h of exposure to 0.3 mM Zn2+ and 0.03-0.1 mM Cd2+
expression of PCS2 is induced in root, stem, and leaf tissues within 24 h of exposure to 0.3 mM Zn2+ and 0.03-0.1 mM Cd2+
expression patterns of AtPCS2 in Arabidopsis thaliana in response to various heavy metals or abiotic stresses, overview
in the developing rice seeds, the Cd exposure significantly upregulates the transcript levels of OsPCS1 (2.5fold). Analysis of the qRT-PCR revealed that the transcript levels of both OsPCS1 and OsPCS2a decreased drastically even after exposure to Cd stress
L-buthionine-sulfoximine can inhibit isoform PCS1 expression in roots, stems and leaves
phytochelatin synthase is constitutively expressed
the expression is significantly induced by cadmium and by abscisic acid
the expression of OsPCS2 is not significantly affected by As(III) stress in the roots
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
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the expression pattern of OsPCS1 splice variants is not changed by Cd or As stress in both shoots and roots
the PCS gene in Chlamydomonas acidophila shows very strong induction by cadmium
the PCS gene in Dunaliella acidophila is not induced by cadmium, most likely due to gene duplication
the two transcript isoforms (OsPCS2a and OsPCS2b) of OsPCS2 gene demonstrate contrasting expression pattern upon Cd stress. The OsPCS2a mRNA level remains almost unaltered in case of the root tissues, but profoundly increased (2.5-15.6folds) between 3 and 72 h in shoot tissues. On the other hand, the amount of OsPCS2b transcript is significantly enhanced with maximum expression maintained between 12 and 72 h in roots, but is significantly downregulated in shoots until 72 h, when its expression rapidly increased to about 4.5fold upon Cd treatment. In the developing rice seeds, the Cd exposure significantly upregulates the transcript levels of OsPCS2a (about 6fold), whereas the mRNA level of OsPCS2b is reduced by about 25%. Analysis of the qRT-PCR revealed that the transcript levels of both OsPCS1 and OsPCS2a decreased drastically even after exposure to Cd stress
there is no significant change in transcript accumulation of PCS1 following Cd2+ treatment
up-regulated under cadmium stress conditions
expression of AtPCS2 is significantly decreased in response to high concentrations of metals Ni2+ (0.1 mM), Mg2+ (1.0 mM), Cd2+ (0.3 mM), Hg2+ (0.030 mM), Zn2+ (0.5 mM), and Pb2+ (0.5 mM), as well as by abscisic acid (0.1 mM), PEG (15%) drougth, and cold (4C) stress, overview
expression of AtPCS2 is significantly decreased in response to high concentrations of metals Ni2+ (0.1 mM), Mg2+ (1.0 mM), Cd2+ (0.3 mM), Hg2+ (0.030 mM), Zn2+ (0.5 mM), and Pb2+ (0.5 mM), as well as by abscisic acid (0.1 mM), PEG (15%) drougth, and cold (4C) stress, overview
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expression of AtPCS2 is significantly increased in response to 100 and 200 mM NaCl treatment. In addition, transgenic Arabidopsis subjected to salt stress exhibit enhanced proline accumulation and reduced Na+/K+ ratios compared to wild-type plants. The enzyme expression is also induced by H2O2 at 20 mM
expression of AtPCS2 is significantly increased in response to 100 and 200 mM NaCl treatment. In addition, transgenic Arabidopsis subjected to salt stress exhibit enhanced proline accumulation and reduced Na+/K+ ratios compared to wild-type plants. The enzyme expression is also induced by H2O2 at 20 mM
-
-
expression patterns of AtPCS2 in Arabidopsis thaliana in response to various heavy metals or abiotic stresses, overview
expression patterns of AtPCS2 in Arabidopsis thaliana in response to various heavy metals or abiotic stresses, overview
-
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in the developing rice seeds, the Cd exposure significantly upregulates the transcript levels of OsPCS1 (2.5fold). Analysis of the qRT-PCR revealed that the transcript levels of both OsPCS1 and OsPCS2a decreased drastically even after exposure to Cd stress
in the developing rice seeds, the Cd exposure significantly upregulates the transcript levels of OsPCS1 (2.5fold). Analysis of the qRT-PCR revealed that the transcript levels of both OsPCS1 and OsPCS2a decreased drastically even after exposure to Cd stress
-
-
phytochelatin synthase is constitutively expressed
the PCS gene in Chlamydomonas acidophila shows very strong induction by cadmium
-
the PCS gene in Chlamydomonas acidophila shows very strong induction by cadmium
-
-
the PCS gene in Dunaliella acidophila is not induced by cadmium, most likely due to gene duplication
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the PCS gene in Dunaliella acidophila is not induced by cadmium, most likely due to gene duplication
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-
the two transcript isoforms (OsPCS2a and OsPCS2b) of OsPCS2 gene demonstrate contrasting expression pattern upon Cd stress. The OsPCS2a mRNA level remains almost unaltered in case of the root tissues, but profoundly increased (2.5-15.6folds) between 3 and 72 h in shoot tissues. On the other hand, the amount of OsPCS2b transcript is significantly enhanced with maximum expression maintained between 12 and 72 h in roots, but is significantly downregulated in shoots until 72 h, when its expression rapidly increased to about 4.5fold upon Cd treatment. In the developing rice seeds, the Cd exposure significantly upregulates the transcript levels of OsPCS2a (about 6fold), whereas the mRNA level of OsPCS2b is reduced by about 25%. Analysis of the qRT-PCR revealed that the transcript levels of both OsPCS1 and OsPCS2a decreased drastically even after exposure to Cd stress
the two transcript isoforms (OsPCS2a and OsPCS2b) of OsPCS2 gene demonstrate contrasting expression pattern upon Cd stress. The OsPCS2a mRNA level remains almost unaltered in case of the root tissues, but profoundly increased (2.5-15.6folds) between 3 and 72 h in shoot tissues. On the other hand, the amount of OsPCS2b transcript is significantly enhanced with maximum expression maintained between 12 and 72 h in roots, but is significantly downregulated in shoots until 72 h, when its expression rapidly increased to about 4.5fold upon Cd treatment. In the developing rice seeds, the Cd exposure significantly upregulates the transcript levels of OsPCS2a (about 6fold), whereas the mRNA level of OsPCS2b is reduced by about 25%. Analysis of the qRT-PCR revealed that the transcript levels of both OsPCS1 and OsPCS2a decreased drastically even after exposure to Cd stress
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
reduction of the level of arsenic (As) in rice grains is an important challenge for agriculture. Phytochelatin synthase OsPCS1 plays a crucial role in reducing arsenic levels in rice grains. Transgenic plants highly expressing OsPCS1 show significantly lower As levels in grains compared to wild-type plants. PCS1 is a good candidate tool to reduce As levels in rice grains
analysis
biotechnology
environmental protection
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yeast cells expressing AtPCS can be used as an inexpensive sorbent for the removal of toxic arsenic
synthesis
effective conversion of GSH to gamma-glutamylcysteine in repeated batch conversion reactions, at 25°C and using cellulose sponges and microcrystalline cellulose as immobilization carriers. Using PCS immobilized on the cellulose sponge and microcrystalline cellulose, 305 mg and 291 mg gamma-glutamylcysteine, respectively, can be obtained in a 5 mL reaction over five repeated batch reactions
analysis
a HPLC method for the analysis of the activity of phytochelatin synthase is developed
analysis
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use of PCS as a marker for the detection of human Schistosoma japonicum infection. In schistosomiasis japonica positive blood serum samples, tested by enzyme-linked immunosorbent assay, PCS is detected in more positive samples and has fewer cross-reactions than phosphoglycerate mutase, giving 85.05% sensitivity and 93.55% specificity
biotechnology
SrPCS1 has potential applications in genetic engineering of plants for enhancing heavy metal tolerance and phytoremediation of contaminated soils
biotechnology
SrPCS3 has potential applications in genetic engineering of plants for enhancing heavy metal tolerance and phytoremediation of contaminated soils
biotechnology
enhanced biosynthesis of cadmium(II)-selenide (CdS) nanoparticles (NPs) through Arabidopsis thaliana phytochelatin synthase-modified Escherichia coli with fluorescence effect in detection of pyrogallol and gallic acid. CdS NPs act as a classical II-VI semiconductor with various interesting properties and incomparable advantages. Enzyme PCS can effectively capture and enrich Cd2+ so that the generation and subsequent application process of CdS NPs will be greatly improved. A direct detection method based on such CdS NPs is established for determination of pyrogallol and gallic acid, two organic molecules with multiple advantages and wide applications. The method provides an excellent alternative to traditional chemosynthesis and quantitative analysis, which also displays great potential for technological improvement towards green synthesis and application. Method development and evaluation, detailed overview
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REF.
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TITLE
JOURNAL
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YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Arabidopsis thaliana
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96
7110-7115
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Arabidopsis thaliana (Q9S7Z3), Arabidopsis thaliana
brenda
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Characterization of phytochelatin synthase from tomato
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101
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1997
Solanum lycopersicum
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6838-6842
1989
Silene vulgaris, Podophyllum peltatum, Eschscholzia californica, Beta vulgaris, Equisetum giganteum
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Arabidopsis thaliana
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Arabidopsis thaliana (Q9S7Z3)
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903-910
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Arabidopsis thaliana
-
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218
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Schizosaccharomyces pombe, Arabidopsis thaliana
brenda
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Arabidopsis thaliana (Q9S7Z3), Nostoc sp., Nostoc sp. PCC 7120
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223
180-190
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Arabidopsis thaliana
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225
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Arabidopsis thaliana
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598-604
2009
Tetrahymena thermophila (Q4PJK2), Tetrahymena thermophila, Tetrahymena thermophila SB1969 (Q4PJK2)
brenda
Li, A.M.; Yu, B.Y.; Chen, F.H.; Gan, H.Y.; Yuan, J.G.; Qiu, R.; Huang, J.C.; Yang, Z.Y.; Xu, Z.F.
Characterization of the Sesbania rostrata phytochelatin synthase gene: Alternative splicing and function of four isoforms
Int. J. Mol. Sci.
10
3269-3282
2009
Sesbania rostrata (C7DSA8), Sesbania rostrata (Q1L734), Sesbania rostrata (C7DSA6), Sesbania rostrata (C7DSA3), Sesbania rostrata
brenda
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)
brenda
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
brenda
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 (Q9S7Z3), Arabidopsis thaliana
brenda
Liu, Z.; Gu, C.; Chen, F.; Yang, D.; Wu, K.; Chen, S.; Jiang, J.; Zhang, Z.
Heterologous expression of a Nelumbo nucifera phytochelatin synthase gene enhances cadmium tolerance in Arabidopsis thaliana
Appl. Biochem. Biotechnol.
166
722-734
2012
Nelumbo nucifera
brenda
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
brenda
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
brenda
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
brenda
Rea, P.A.
Phytochelatin synthase: of a protease a peptide polymerase made
Physiol. Plant.
145
154-164
2012
Arabidopsis thaliana
brenda
Liu, G.Y.; Zhang, Y.X.; Chai, T.Y.
Phytochelatin synthase of Thlaspi caerulescens enhanced tolerance and accumulation of heavy metals when expressed in yeast and tobacco
Plant Cell Rep.
30
1067-1076
2011
Noccaea caerulescens
brenda
Shukla, D.; Kesari, R.; Mishra, S.; Dwivedi, S.; Tripathi, R.D.; Nath, P.; Trivedi, P.K.
Expression of phytochelatin synthase from aquatic macrophyte Ceratophyllum demersum L. enhances cadmium and arsenic accumulation in tobacco
Plant Cell Rep.
31
1687-1699
2012
Ceratophyllum demersum (E5GCW5), Ceratophyllum demersum
brenda
Chang, Y.; Li, H.; Cong, Y.; Lin, J.; Sheng, B.
Characterization and Expression of a phytochelatin synthase gene in birch-leaf pear (Pyrus betulaefolia Bunge)
Plant Mol. Biol. Rep.
30
1329-1337
2012
Pyrus betulifolia (H2DFA2)
-
brenda
Meyer, C.L.; Peisker, D.; Courbot, M.; Craciun, A.R.; Cazale, A.C.; Desgain, D.; Schat, H.; Clemens, S.; Verbruggen, N.
Isolation and characterization of Arabidopsis halleri and Thlaspi caerulescens phytochelatin synthases
Planta
234
83-95
2011
Arabidopsis halleri (F1KLT6), Arabidopsis halleri (Q56VL5), Arabidopsis halleri, Noccaea caerulescens (B3FMV8), Noccaea caerulescens (Q698X7), Noccaea caerulescens
brenda
Li, H.; Cong, Y.; Lin, J.; Chang, Y.
Enhanced tolerance and accumulation of heavy metal ions by engineered Escherichia coli expressing Pyrus calleryana phytochelatin synthase
J. Basic Microbiol.
55
398-405
2015
Pyrus calleryana
brenda
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 (Q9S7Z3), Arabidopsis thaliana
brenda
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 (Q9S7Z3), Arabidopsis thaliana
brenda
Garcia-Garcia, J.D.; Girard, L.; Hernandez, G.; Saavedra, E.; Pardo, J.P.; Rodriguez-Zavala, J.S.; Encalada, R.; Reyes-Prieto, A.; Mendoza-Cozatl, D.G.; Moreno-Sanchez, R.
Zn-bis-glutathionate is the best co-substrate of the monomeric phytochelatin synthase from the photosynthetic heavy metal-hyperaccumulator Euglena gracilis
Metallomics
6
604-616
2014
Euglena gracilis (A0A075TCK5), Euglena gracilis
brenda
Fan, W.; Guo, Q.; Liu, C.; Liu, X.; Zhang, M.; Long, D.; Xiang, Z.; Zhao, A.
Two mulberry phytochelatin synthase genes confer zinc/cadmium tolerance and accumulation in transgenic Arabidopsis and tobacco
Gene
645
95-104
2018
Morus notabilis (W9QSJ2), Morus notabilis (W9QSW3), Morus notabilis
brenda
Bellini, E.; Maresca, V.; Betti, C.; Castiglione, M.R.; Fontanini, D.; Capocchi, A.; Sorce, C.; Borso, M.; Bruno, L.; Sorbo, S.; Basile, A.; Sanita di Toppi, L.
The moss Leptodictyum riparium counteracts severe cadmium stress by activation of glutathione transferase and phytochelatin synthase, but slightly by phytochelatins
Int. J. Mol. Sci.
21
1583
2020
Leptodictyum riparium
brenda
Li, M.; Stragliati, L.; Bellini, E.; Ricci, A.; Saba, A.; Sanita di Toppi, L.; Varotto, C.
Evolution and functional differentiation of recently diverged phytochelatin synthase genes from Arundo donax L.
J. Exp. Bot.
70
5391-5405
2019
Arundo donax (A0A4Y5QLU9), Arundo donax (A0A4Y5QPE2), Arundo donax (A0A4Y5QLV0), Arundo donax
brenda
Shah, K.; King, G.D.; Jiang, H.
A chromatin modulator sustains self-renewal and enables differentiation of postnatal neural stem and progenitor cells
J. Mol. Cell Biol.
12
4-16
2020
Oryza sativa Japonica Group (A0A1Q2SVY7), Oryza sativa Japonica Group (Q0DI55)
brenda
Kim, Y.O.; Kang, H.; Ahn, S.J.
Overexpression of phytochelatin synthase AtPCS2 enhances salt tolerance in Arabidopsis thaliana
J. Plant Physiol.
240
153011
2019
Arabidopsis thaliana (A0A1P8AVN4), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (A0A1P8AVN4)
brenda
Olsson, S.; Penacho, V.; Puente-Sanchez, F.; Diaz, S.; Gonzalez-Pastor, J.E.; Aguilera, A.
Horizontal gene transfer of phytochelatin synthases from bacteria to extremophilic green algae
Microb. Ecol.
73
50-60
2017
Dunaliella acidophila, Chlamydomonas acidophila, Dunaliella acidophila RT5, Chlamydomonas acidophila RT46
brenda
Park, H.C.; Hwang, J.E.; Jiang, Y.; Kim, Y.J.; Kim, S.H.; Nguyen, X.C.; Kim, C.Y.; Chung, W.S.
Functional characterisation of two phytochelatin synthases in rice (Oryza sativa cv. Milyang 117) that respond to cadmium stress
Plant Biol.
21
854-861
2019
Oryza sativa
brenda
Uraguchi, S.; Tanaka, N.; Hofmann, C.; Abiko, K.; Ohkama-Ohtsu, N.; Weber, M.; Kamiya, T.; Sone, Y.; Nakamura, R.; Takanezawa, Y.; Kiyono, M.; Fujiwara, T.; Clemens, S.
Phytochelatin synthase has contrasting effects on cadmium and arsenic accumulation in rice grains
Plant Cell Physiol.
58
1730-1742
2017
Oryza sativa Japonica Group (A0A1Q2SVY7), Oryza sativa Japonica Group (Q0DI55), Oryza sativa Japonica Group (B7EJX7), Oryza sativa Japonica Group (Q5VRI1), Oryza sativa Japonica Group (A0A224ASC9)
brenda
Hayashi, S.; Kuramata, M.; Abe, T.; Takagi, H.; Ozawa, K.; Ishikawa, S.
Phytochelatin synthase OsPCS1 plays a crucial role in reducing arsenic levels in rice grains
Plant J.
91
840-848
2017
Oryza sativa Japonica Group (A0A1Q2SVY7), Oryza sativa Japonica Group (Q0DI55)
brenda
Das, N.; Bhattacharya, S.; Bhattacharyya, S.; Maiti, M.K.
Identification of alternatively spliced transcripts of rice phytochelatin synthase 2 gene OsPCS2 involved in mitigation of cadmium and arsenic stresses
Plant Mol. Biol.
94
167-183
2017
Oryza sativa Indica Group (Q8GZR3), Oryza sativa Indica Group (A0A1B2LVE0), Oryza sativa Indica Group, Oryza sativa Indica Group IR64 (Q8GZR3), Oryza sativa Indica Group IR64 (A0A1B2LVE0)
brenda
Fontanini, D.; Andreucci, A.; Ruffini Castiglione, M.; Basile, A.; Sorbo, S.; Petraglia, A.; Degola, F.; Bellini, E.; Bruno, L.; Varotto, C.; Sanita di Toppi, L.
The phytochelatin synthase from Nitella mucronata (Charophyta) plays a role in the homeostatic control of iron(II)/(III)
Plant Physiol. Biochem.
127
88-96
2018
Nitella mucronata
brenda
Chaurasia, N.; Mishra, Y.; Chatterjee, A.; Rai, R.; Yadav, S.; Rai, L.C.
Overexpression of phytochelatin synthase (pcs) enhances abiotic stress tolerance by altering the proteome of transformed Anabaena sp. PCC 7120
Protoplasma
254
1715-1724
2017
Nostoc sp. PCC 7120 = FACHB-418 (Q8YY76)
brenda
Zhang, D.; Yamamoto, T.; Tang, D.; Kato, Y.; Horiuchi, S.; Ogawa, S.; Yoshimura, E.; Suzuki, M.
Enhanced biosynthesis of CdS nanoparticles through Arabidopsis thaliana phytochelatin synthase-modified Escherichia coli with fluorescence effect in detection of pyrogallol and gallic acid
Talanta
195
447-455
2019
Arabidopsis thaliana (Q9S7Z3), Arabidopsis thaliana
brenda
Nakai, T.; Hirata, K.; Nagano, K.; Arai, M.; Uyama, H.; Hirata, Y.; Muraoka, M.
Effective repeated production of gamma-glutamylcysteine, essential for intracellular glutathione production, using cellulose-immobilized phytochelatin synthase-like enzyme NsPCS
Appl. Biochem. Biotechnol.
197
3258-3270
2025
Nostoc sp. PCC 7120 = FACHB-418 (Q8YY76)
brenda
Azizi, N.; Shahpiri, A.
Functional characterization of Helianthus annuus phytochelatin synthase (HaPCS) Gene expression and protein profiles of HaPCS responding to arsenic and evaluation of arsenic accumulation in engineered bacteria expressing HaPCS
Environ. Exp. Bot.
187
104470
2021
Helianthus annuus (A0A251UGN0)
-
brenda
Zhu, S.; Shi, W.; Jie, Y.
Overexpression of BnPCS1, a novel phytochelatin synthase gene from Ramie (Boehmeria nivea), enhanced Cd tolerance, accumulation, and translocation in Arabidopsis thaliana
Front. Plant Sci.
12
639189
2021
Boehmeria nivea (V9VLL7)
brenda
Wu, C.; Zhang, J.; Chen, M.; Liu, J.; Tang, Y.
Characterization of a Nicotiana tabacum phytochelatin synthase 1 and its response to cadmium stress
Front. Plant Sci.
15
1418762
2024
Nicotiana tabacum (Q84UY7)
brenda
Diaz, S.; Aguilera, A.; de Figueras, C.G.; de Francisco, P.; Olsson, S.; Puente-Sanchez, F.; Gonzalez-Pastor, J.E.
Heterologous expression of the phytochelatin synthase CaPCS2 from Chlamydomonas acidophila and its effect on different stress factors in Escherichia coli
Int. J. Environ. Res. Public Health
19
7692
2022
Chlamydomonas acidophila
brenda
Xing, Q.; Hasan, M.K.; Li, Z.; Yang, T.; Jin, W.; Qi, Z.; Yang, P.; Wang, G.; Ahammed, G.J.; Zhou, J.
Melatonin-induced plant adaptation to cadmium stress involves enhanced phytochelatin synthesis and nutrient homeostasis in Solanum lycopersicum L
J. Hazard. Mater.
456
131670
2023
Solanum lycopersicum (A0A3Q7I4L4)
brenda
Angeles, J.M.M.; Goto, Y.; Trinh, M.A.D.; Rivera, P.T.; Villacorte, E.A.; Kawazu, S.I.
Serological evaluation of the schistosomes secretory enzyme phytochelatin synthase and phosphoglycerate mutase for the detection of human Schistosoma japonicum infection
Parasitol. Res.
121
2445-2448
2022
Schistosoma japonicum
brenda
Inoue, R.; Nakamura, N.; Matsumoto, C.; Takase, H.; Sekiya, J.; Prieto, R.
Characterization of gamma-glutamyltransferase- and phytochelatin synthase-mediated catabolism of glutathione and glutathione S-conjugates in Arabidopsis thaliana
Plant Biotechnol.
39
381-389
2022
Arabidopsis thaliana (Q9S7Z3)
brenda
Su, H.; Zou, T.; Lin, R.; Zheng, J.; Jian, S.; Zhang, M.
Characterization of a phytochelatin synthase gene from Ipomoea pes-caprae involved in cadmium tolerance and accumulation in yeast and plants
Plant Physiol. Biochem.
155
743-755
2020
Ipomoea pes-caprae (A0A223A4L4)
brenda
Chen, Y.; Yang, J.; Zhao, X.; Sun, Z.; Li, G.; Hussain, S.; Li, X.; Zhang, L.; Wang, Z.; Gong, H.; Hou, H.
Effects of SpGSH1 and SpPCS1 overexpression or co-overexpression on cadmium accumulation in yeast and Spirodela polyrhiza
Plant Physiol. Biochem.
216
109097
2024
Spirodela polyrhiza
brenda
Bellini, E.; Varotto, C.; Borso, M.; Rugnini, L.; Bruno, L.; Sanita di Toppi, L.
Eukaryotic and prokaryotic phytochelatin synthases differ less in functional terms than previously thought A comparative analysis of Marchantia polymorpha and Geitlerinema sp. PCC 7407
Plants (Basel)
9
914
2020
Marchantia polymorpha subsp. ruderalis (A0A176VFF5), Geitlerinema sp. PCC 7407 (K9S8X3)
brenda
Liu, J.; Zhang, J.; Kim, S.H.; Lee, H.S.; Marinoia, E.; Song, W.Y.
Characterization of Brassica rapa metallothionein and phytochelatin synthase genes potentially involved in heavy metal detoxification
PLoS ONE
16
e0252899
2021
Brassica rapa subsp. oleifera
brenda
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