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Information on EC 6.3.2.3 - glutathione synthase and Organism(s) Synechocystis sp. and UniProt Accession P73493
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EC Tree
6.3.2.3 glutathione synthaseSpecify your search results
Word Map
- 6.3.2.3
- gamma-glutamylcysteine
- dismutase
-
gamma-glutamyl
- catalase
- s-transferase
- sulfoximine
- cadmium
-
5-oxoprolinuria
-
buthionine
- 5-oxoproline
-
hemolytic
- acidosis
- phytochelatins
- transpeptidase
- gamma-gcs
-
school
-
school-based
-
pyroglutamic
-
glutathione-related
-
atp-grasp
-
bullied
-
l-buthionine-s,r-sulfoximine
- juncea
-
6.3.2.2
-
glutathione-deficient
-
homoglutathione
-
gsh-dependent
- medicine
- biotechnology
- synthesis
- analysis
The taxonomic range for the selected organisms is: Synechocystis sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glutathione synthetase, glutathione synthase, gsh synthetase, gshs, gsh-s, gsh synthase, tags2, gshii, gshs1, tags1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Glutathione synthase
-
-
-
-
Glutathione synthetase
-
-
-
-
Glutathione synthetase (tripeptide)
-
-
-
-
GSH synthetase
-
-
-
-
GSHase
-
-
-
-
GSS
-
-
-
-
Phytochelatin synthetase
-
-
-
-
Synthetase, glutathione
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
random ter-reactant reaction mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxamide formation
-
-
-
-
carboxylic acid-amide formation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
gamma-L-glutamyl-L-cysteine:glycine ligase (ADP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9023-62-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
product inhibition, competitive versus ATP, noncompetitive versus gamma-L-glutamyl-L-cysteine and glycine
glutathione
product inhibition, noncompetitive versus ATP, gamma-L-glutamyl-L-cysteine, and glycine
phosphate
product inhibition, noncompetitive versus ATP, gamma-L-glutamyl-L-cysteine, and glycine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics and kinetic mechanism, overview
-
additional information
additional information
-
steady-state kinetics and kinetic mechanism, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Synechocystis glutathione synthase shares properties with other prokaryotic enzymes
physiological function
physiological function
isolation of fully segregated gshB deletion mutants. The mutant strain lacks reduced glutathione but instead accumulates the precursor compound gamma-glutamylcysteine. The deletion strain grows slower than the wild-type strain under favorable conditions and exhibits extremely reduced growth or death when subjected to conditions promoting oxidative stress. After subjecting the strains to multiple environmental and redox perturbations, we found that conditions promoting growth stimulate glutathione biosynthesis. Cellular GSH and gamma-glutamylcysteine content decline following exposure to dark and blue light and during photoheterotrophic growth. A rapid depletion of GSH and gamma-glutamylcysteine is observed in the wild type and the mutant strain, when cells are starved for nitrate or sulfate
physiological function
glutathione biosynthesis catalysed by glutamate-cysteine ligase, EC 6.3.2.2, and glutathione synthetase is essential for maintaining redox homoeostasis and protection against oxidative damage in diverse eukaroytes and bacteria
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutants from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gshB, expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cameron, J.C.; Pakrasi, H.B.
Essential role of glutathione in acclimation to environmental and redox perturbations in the cyanobacterium Synechocystis sp. PCC 6803
Plant Physiol.
154
1672-1685
2010
Synechocystis sp. (P73493), Synechocystis sp.
Musgrave, W.B.; Yi, H.; Kline, D.; Cameron, J.C.; Wignes, J.; Dey, S.; Pakrasi, H.B.; Jez, J.M.
Probing the origins of glutathione biosynthesis through biochemical analysis of glutamate-cysteine ligase and glutathione synthetase from a model photosynthetic prokaryote
Biochem. J.
450
63-72
2013
Synechocystis sp. (P73493), Synechocystis sp.
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Release 2023.1 (January 2023)
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