2.3.2.15: glutathione gamma-glutamylcysteinyltransferase
This is an abbreviated version!
For detailed information about glutathione gamma-glutamylcysteinyltransferase, go to the full flat file.
Word Map on EC 2.3.2.15
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2.3.2.15
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phytochelatins
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neurogenesis
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cadmium
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subventricular
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oligodendrocyte
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neurospheres
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hippocampal
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gsh
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neurogenic
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arsenic
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self-renewal
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phytoremediation
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metallothioneins
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nestin
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multipotent
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asiii
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subgranular
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neuroblast
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metalloid
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cord-derived
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analysis
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agriculture
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biotechnology
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environmental protection
- 2.3.2.15
- phytochelatins
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neurogenesis
- cadmium
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subventricular
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oligodendrocyte
-
neurospheres
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hippocampal
- gsh
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neurogenic
- arsenic
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self-renewal
-
phytoremediation
- metallothioneins
- nestin
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multipotent
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asiii
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subgranular
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neuroblast
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metalloid
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cord-derived
- analysis
- agriculture
- biotechnology
- environmental protection
Reaction
Synonyms
AdPCS1, AdPCS2, AdPCS3, alr0975, AtPCS, AtPCS1, AtPCS2, AtPCSI, BjPCS1, CaPCS1, CaPCS2, CePCS, DaPCS1, gamma-EC dipeptidyl(trans)peptidase, gamma-glutamyl-cysteine transpeptidase, gamma-glutamylcysteine dipeptidyl transpeptidase, gamma-glutamylcysteine transpeptidase, gamma-glutamylcysteinyl dipeptidyl transpeptidase, gamma-glutamylcysteinyl transpeptidase, glutathione gamma-glutamylcysteinyltransferase, LjPCS1, LjPCS3, MnPCS1, MnPCS2, NsPCS, OsPCS1, OsPCS15, OsPCS1a, OsPCS1b, OsPCS1c, OsPCS1full, OsPCS2, OsPCS5, PC synthase, PCS, PCS1, PCS15, PCS2, PCS5, phytochelatin synthase, phytochelatin synthase 1, phytochelatin synthase 2, phytochelatin synthase1, pPhytochelatin synthase, pseudo-phytochelatin synthase, SrPCS, SrPCS1, SrPCS2, SrPCS3, SrPCS4, TtpsiPCS
ECTree
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General Information on EC 2.3.2.15 - glutathione gamma-glutamylcysteinyltransferase
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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
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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
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
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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
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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
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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
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evolution
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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
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evolution
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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
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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
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
RNAi-mediated grain-specific silencing of OsPCS decreases cadmium accumulation in rice grain
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
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 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
transgenic plants highly expressing OsPCS1 show significantly lower As levels in grains than do wild-type plants
malfunction
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RNAi-mediated grain-specific silencing of OsPCS decreases cadmium accumulation in rice grain
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malfunction
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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. 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
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physiological function
phytochelatins play an important role in detoxification of heavy metals in plants
physiological function
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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
enhanced metal (Cd2+ and As5+) accumulation is due to post-translational activation of the enzyme in the presence of Cd2+ ion
physiological function
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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
the enzyme is involved in cellular cadmium tolerance
physiological function
the enzyme is involved in cellular cadmium tolerance
physiological function
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the enzyme is involved in the response of Nelumbo nucifera to cadmium stress
physiological function
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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
the enzyme binds, localizes, stores or sequesters heavy metals in plant cells
physiological function
the enzyme confers resistance on Cd2+ stress
physiological function
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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
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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
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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
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 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 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 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 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 OsPCS1 plays a crucial role in reducing arsenic levels in rice grains. Redundancy between OsPCS1 and OsPCS2
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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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
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
redundancy between OsPCS1 and OsPCS2
physiological function
role of of enzyme PCS in abiotic stress tolerance
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
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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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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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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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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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