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Information on EC 6.3.2.3 - glutathione synthase and Organism(s) Homo sapiens and UniProt Accession P48637
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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: Homo sapiens
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
-
-
-
-
additional information
the enzyme belongs to the glutathione synthetase ATP-binding domain-like superfamily
Glutathione synthase
-
-
-
-
Glutathione synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
mechanism, active site residues are Glu144, Asn146, Lys305, and Lys364, interaction of these residues with the ligands is essential for enzyme activity, especially Glu144 seems to be very important for stabilization of the reaction intermediate, but the active site residues are not essential for the overall enzyme structure
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 + L-gamma-glutamyl-L-alpha-aminobutyrate + glycine
ADP + L-gamma-glutamyl-L-alpha-aminobutyryl-glycine
gamma-GluABA, an analogue of gamma-L-glutamyl-L-cysteine (gamma-GC) with the same activity and kinetic properties as gamma-GC
-
-
?
ATP + gamma-Glu-2-aminobutyrate + hydroxylamine
ADP + phosphate + gamma-(alpha-aminomethyl)Glu-2-aminobutyryl-Gly
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-Glu-aminobutanoate + Gly
ADP + phosphate + ophthalmic acid
-
-
-
-
?
glycine + ATP + gamma-L-glutamyl-L-cysteine
ADP + phosphate + glutathione
-
assay at pH 8.2
-
-
?
additional information
?
-
-
dysregulation of GSH synthesis occurs in aging and is increasingly being recognized as contributing to the pathogenesis of many pathological conditions including diabetes mellitus, pulmonary fibrosis, cholestatic liver injury, endotoxemia and drug-resistant tumor cells, detailed overview. Decrease in the activity of GS alone without a change in glutathione cysteine ligase, GCL EC 6.3.2.2, and a fall in muscle GSH levels occur after surgical trauma in human skeletal muscle
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
patients with hereditary glutathione synthetase deficiency suffer from haemolytic anaemia, 5-oxoprolinuria, metabolic acidosis, recurrent bacterial infections and various degrees of central nervous system dysfunction
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
two NFE2 sites in the human GSS promoter play important roles in the basal expression of glutathione synthetase. The glutathione synthetase gene expression is also regulated by Nrf2
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
wild-type enzyme shows negative cooperativity
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
second step in the biosynthesis of glutahione
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
gamma-glutamyl-cysteine is bound cooperatively by the enzyme, ATP might play a key role in sequential binding, but its amount does not alter the cooperative binding of gamma-glutamyl-cysteine
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
inpresence of dithiothreitol
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
final step of glutathione biosynthesis
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
glutathione is a ubiquitous intracellular peptide with diverse functions that include detoxification, antioxidant defense, maintenance of thiol status, and modulation of cell proliferation, whose biosynthesis is tightly regulated, overview. GSH synthase is regulated in a coordinated manner and its up-regulation can further enhance the capacity of the cell to synthesize GSH, enzyme regulation, detailed overview
-
-
?
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-Glu-L-Cys + Gly
ADP + phosphate + glutathione
second step in the biosynthesis of glutahione
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
glutathione is a ubiquitous intracellular peptide with diverse functions that include detoxification, antioxidant defense, maintenance of thiol status, and modulation of cell proliferation, whose biosynthesis is tightly regulated, overview. GSH synthase is regulated in a coordinated manner and its up-regulation can further enhance the capacity of the cell to synthesize GSH, enzyme regulation, detailed overview
-
-
?
additional information
?
-
-
dysregulation of GSH synthesis occurs in aging and is increasingly being recognized as contributing to the pathogenesis of many pathological conditions including diabetes mellitus, pulmonary fibrosis, cholestatic liver injury, endotoxemia and drug-resistant tumor cells, detailed overview. Decrease in the activity of GS alone without a change in glutathione cysteine ligase, GCL EC 6.3.2.2, and a fall in muscle GSH levels occur after surgical trauma in human skeletal muscle
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
patients with hereditary glutathione synthetase deficiency suffer from haemolytic anaemia, 5-oxoprolinuria, metabolic acidosis, recurrent bacterial infections and various degrees of central nervous system dysfunction
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
two NFE2 sites in the human GSS promoter play important roles in the basal expression of glutathione synthetase. The glutathione synthetase gene expression is also regulated by Nrf2
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
final step of glutathione biosynthesis
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
decrease of enzyme activity in hypoxia: 20% after 6 h, 17% after 12 h, 23% after 24 h, hypoxia-induced decrease in enzyme activity may be prevented by MAPK inhibition and catalase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Thioacetamide
-
increases the enzyme expression and activity in Chang cells by 50% at 6.66 mM
additional information
-
oxidative stress induces the enzyme, key transcription factors include Nrf2/Nrf1 via the antioxidant response element, ARE, activator protein-1, AP-1, and nuclear factor kappa B, NFkappaB. Nrf1 and Nrf2 overexpression induces the human GS promoter activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
gamma-L-Glu-aminobutanoate
-
mutant G371V, 37°C, pH not specified in the publication
0.89
gamma-L-Glu-aminobutanoate
-
mutant G369V, 37°C, pH not specified in the publication
1.26
gamma-L-Glu-aminobutanoate
-
wild-type, 37°C, pH not specified in the publication
additional information
additional information
kinetics, substrate and ligand binding, wild-type enzyme and mutants
-
additional information
additional information
-
kinetics, substrate and ligand binding, wild-type enzyme and mutants
-
additional information
additional information
-
kinetics of cooperative substrate binding
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
patients with genetic deficiencies in hGS suffer from a variety of symptoms, most notably hemolytic anemia and neurological disorders. Deficiencies of GSH are associated with a variety of diseases including Parkinson's disease, Alzheimer's disease, Lou Gehrig's disease, diabetes, cystic fibrosis, and HIV/AIDS. In the R221A mutant, the interchain salt bridge and hydrogen bonds between R221 and D24 are broken, and a new salt bridge forms between R34 and D24
physiological function
regulation of hGS plays a critical role in maintaining the cellular glutathione levels required to relieve oxidative stress
additional information
additional information
the active site is composed of three highly conserved catalytic loops, notably the alanine rich A-loop, Asp458 is important for cooperativity and active site structure, it impacts the allostery of the enzyme. Asp458 is important for loop closure and is a critical residue within the enzyme's A-loop. Enzyme structure-function modeling, molecular dynamics, overview
additional information
-
the active site is composed of three highly conserved catalytic loops, notably the alanine rich A-loop, Asp458 is important for cooperativity and active site structure, it impacts the allostery of the enzyme. Asp458 is important for loop closure and is a critical residue within the enzyme's A-loop. Enzyme structure-function modeling, molecular dynamics, overview
additional information
the obligate homodimer human glutathione synthetase (hGS) provides an ideal system for exploring the role of protein-protein interactions in the structural stability, activity and allostery of enzymes. The two subunits interact at a relatively small dimer interface dominated by electrostatic interactions between residues S42, R221, and D24, these residues are crucial to function of hGS. While the ionic hydrogen bonds and salt bridges between S42, R221, and D24 do not mediate allosteric communication in hGS, these interactions have a dramatic impact on the activity and structural stability of the enzyme, molecular dynamics simulations, overview. Since D24 participates in two significant interactions (a salt bridge with R221 and an ionic hydrogen bond with S42), this residue plays the largest role in hGS activity and stability. Structure and stability comparisons of wild-type enzyme and mutant enzymes, overview
additional information
-
the obligate homodimer human glutathione synthetase (hGS) provides an ideal system for exploring the role of protein-protein interactions in the structural stability, activity and allostery of enzymes. The two subunits interact at a relatively small dimer interface dominated by electrostatic interactions between residues S42, R221, and D24, these residues are crucial to function of hGS. While the ionic hydrogen bonds and salt bridges between S42, R221, and D24 do not mediate allosteric communication in hGS, these interactions have a dramatic impact on the activity and structural stability of the enzyme, molecular dynamics simulations, overview. Since D24 participates in two significant interactions (a salt bridge with R221 and an ionic hydrogen bond with S42), this residue plays the largest role in hGS activity and stability. Structure and stability comparisons of wild-type enzyme and mutant enzymes, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GSHB_HUMAN
474
0
52385
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
the two active sites of hGS, which are 40 A apart, display allosteric modulation by the substrate gamma-glutamylcysteine (gamma-GC) during the synthesis of glutathione, a key cellular antioxidant. The two subunits interact at a relatively small dimer interface dominated by electrostatic interactions between residues S42, R221, and D24. While the ionic hydrogen bonds and salt bridges between S42, R221, and D24 do not mediate allosteric communication in hGS, these interactions have a dramatic impact on the activity and structural stability of the enzyme. hGS residues S42, R221 and D24 have hydrogen bonding and ionic interactions across the dimer interface decrease activity, maintain negative cooperativity, increase L-gamma-glutamyl-L-alpha-aminobutyrate affinity, and increase catalytic efficiency when mutated to alanine
dimer
additional information
additional information
active site residues are Glu144, Asn146, Lys305, and Lys364, interaction of these residues with the ligands is essential for enzyme activity, especially with Glu144, but they are not essential for the overall enzyme structure
additional information
-
active site residues are Glu144, Asn146, Lys305, and Lys364, interaction of these residues with the ligands is essential for enzyme activity, especially with Glu144, but they are not essential for the overall enzyme structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
computational structure modeling of wild-type and mutant enzymes using crystal structure data at 2.1 A resolution, interactions of actie site residues Glu144, Asn146, Lys305, and Lys364, and ligands ADP2-, SO42-, and Mg2+
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D219A
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 4% of the wild-type activity
D219G
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 27% of the wild-type activity. Negative cooperativity for L-gamma-glutamyl-L-alpha-aminobutyric acid is changed to positive
D24A
site-directed mutagenesis, the mutant shows a slight increase in catalytic efficiency compared to wild-type enzyme
D458A
site-directed mutagenesis, the mutant shows 10% activity compared to the wild-type enzyme
D458N
site-directed mutagenesis, the mutant shows 15% activity compared to the wild-type enzyme
D458R
site-directed mutagenesis, the mutant shows 7% activity compared to the wild-type enzyme
E144A
site-directed mutagenesis, 0.05% activity compared to the wild-type enzyme, unaltered tertiary structure
E144K
site-directed mutagenesis, inactive mutant, unaltered tertiary structure
K305A
site-directed mutagenesis, 6.5% activity compared to the wild-type enzyme, 7fold increased Km for glycine, loss of negative cooperativity, 105fold increased Km for ATP, unaltered tertiary structure
K305E
site-directed mutagenesis, 5% activity compared to the wild-type enzyme, loss of negative cooperativity, 40fold increased Km for ATP, unaltered tertiary structure
K364A
site-directed mutagenesis, 0.1% activity compared to the wild-type enzyme, unaltered tertiary structure
K364E
site-directed mutagenesis, 0.2% activity compared to the wild-type enzyme, unaltered tertiary structure
L188P
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 9% of the wild-type activity
N146A
site-directed mutagenesis, 0.1% activity compared to the wild-type enzyme, unaltered tertiary structure
N146D
site-directed mutagenesis, 0.05% activity compared to the wild-type enzyme, unaltered tertiary structure
N146K
site-directed mutagenesis, inactive mutant, unaltered tertiary structure
R221A
site-directed mutagenesis, the mutant shows a slight increase in catalytic efficiency compared to wild-type enzyme, the R221A mutation also has a large impact on the intrachain bonding structure
R283C
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 13% of the wild-type activity
S42A
site-directed mutagenesis, the mutant shows a slight increase in catalytic efficiency compared to wild-type enzyme
Y208C
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 2% of the wild-type activity
Y270H
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 6% of the wild-type activity
C294A
-
mutant enzymes Cys294Ala and Cys409Ala retain significant residual activity. Substantial decreases in activity are detected with mutant Cys522Ala and Cys-free mutant Cys294/Cys409/Cys422 to Ala294/Ala409/Ala422
C409A
-
mutant enzymes Cys294Ala and Cys409Ala retain significant residual activity. Substantial decreases in activity are detected with mutant Cys522Ala and Cys-free mutant Cys294/Cys409/Cys422 to Ala294/Ala409/Ala422
C522A
-
mutant enzymes Cys294Ala and Cys409Ala retain significant residual activity. Substantial decreases in activity are detected with mutant Cys522Ala and Cys-free mutant Cys294/Cys409/Cys422 to Ala294/Ala409/Ala422
G369V
-
mutation in G-loop glycine triad, about 0.7% of wild-type activity. Mutation decreases ligand binding and prevent active site closure and protection
G370V
-
mutation in G-loop glycine triad, about 0.3% of wild-type activity. Mutation decreases ligand binding and prevent active site closure and protection
V44A/V45A
-
decrease in melting temperature, initial activity similar to wild-type
additional information
additional information
all Asp458 mutants display a change in cooperativity from negative cooperativity to non-cooperative. All mutants show similar stability as compared to wild-type enzyme, differential scanning calorimetry
additional information
-
all Asp458 mutants display a change in cooperativity from negative cooperativity to non-cooperative. All mutants show similar stability as compared to wild-type enzyme, differential scanning calorimetry
additional information
structure and stability comparisons of wild-type enzyme and mutant enzymes, overview
additional information
-
structure and stability comparisons of wild-type enzyme and mutant enzymes, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, when stored in 20 mM Tris-Cl and 1 mM EDTA, pH 8.6, in sterile cryogenic tubes at 4°C, the recombinant hGS dimer interface mutant enzymes lose activity in the 30 hours after purification. Both R221A and D24A lose activity in a biphasic manner within a few hours: D24A loses 30% of activity in 4 hours, while the activity of R221A decreases by 20% in 7.5 hours
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type enzyme from Escherichia coli, to homogeneity
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of N-terminally His-tagged wild-type enzyme in Escherichia coli BL21(DE3)
gene GSS, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain XL1 Blue
seven naturally occurring missense mutations (L188P, D219A, D219G, Y270C, Y270H, R283C and P314L) are expressed using a His-tagged, Escherichia coli-based expression system
cloning of the enzyme promoter and molecular mechanisms of GS transcriptional regulation, overview. Nrf1 and Nrf2 overexpression induces the human GS promoter activity. Human GS promoter contains two regions with homology to the nuclear factor erythroid 2, NFE2, motif that are required for basal activity as mutation of these sites reduces the human GS promoter activity by 66%
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
assay of glutathione synthetase in erythrocytes by HPLC with fluorimetric detection, useful for rapid screening of erythrocytes glutathione synthetase activity in various pathological conditions
medicine
-
the enzyme is a target for therapy of disease like diabetes mellitus, pulmonary fibrosis, cholestatic liver injury, endotoxemia and drug-resistant tumor cells, since manipulation of the GSH synthetic capacity is beneficial in treatment of many of these disorders
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Meister, A.
Glutathione synthesis
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
10
671-697
1974
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Pigeon
-
Nardi, G.; Cipollaro, M.; Loguercio, C.
Assay of gamma-glutamylcysteine synthetase and glutathione synthetase in erythrocytes by high-performance liquid chromatography with fluorimetric detection
J. Chromatogr.
530
122-128
1990
Homo sapiens
Gali, R.R.; Board, P.G.
Identification of an essential cysteine residue in human glutathione synthase
Biochem. J.
321
207-210
1997
Homo sapiens
Gali, R.R.; Board, P.G.
Sequencing and expression of a cDNA for human glutathione synthetase
Biochem. J.
310
353-358
1995
Homo sapiens
Njalsson, R.; Norgren, S.; Larsson, A.; Huang, C.S.; Anderson, M.E.; Luo, J.L.
Cooperative binding of gamma-glutamyl substrate to human glutathione synthetase
Biochem. Biophys. Res. Commun.
289
80-84
2001
Homo sapiens
Huang, Z.A.; Yang, H.; Chen, C.; Zeng, Z.; Lu, S.C.
Inducers of gamma-glutamylcysteine synthetase and their effects on glutathione synthetase expression
Biochim. Biophys. Acta
1493
48-55
2000
Homo sapiens, Rattus norvegicus
Dinescu, A.; Cundari, T.R.; Bhansali, V.S.; Luo, J.L.; Anderson, M.E.
Function of conserved residues of human glutathione synthetase: implications for the ATP-grasp enzymes
J. Biol. Chem.
279
22412-22421
2004
Homo sapiens (P48637), Homo sapiens
Njalsson, R.; Carlsson, K.; Bhansali, V.; Luo, J.L.; Nilsson, L.; Ladenstein, R.; Anderson, M.; Larsson, A.; Norgren, S.
Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
Biochem. J.
381
489-494
2004
Homo sapiens (P48637), Homo sapiens
Lee, T.D.; Yang, H.; Whang, J.; Lu, S.C.
Cloning and characterization of the human glutathione synthetase 5'-flanking region
Biochem. J.
390
521-528
2005
Homo sapiens (P48637), Homo sapiens
Dinescu, A.; Anderson, M.E.; Cundari, T.R.
Catalytic loop motion in human glutathione synthetase: A molecular modeling approach
Biochem. Biophys. Res. Commun.
353
450-456
2007
Homo sapiens
Allen, T.C.; Granville, L.A.; Cagle, P.T.; Haque, A.; Zander, D.S.; Barrios, R.
Expression of glutathione S-transferase pi and glutathione synthase correlates with survival in early stage non-small cell carcinomas of the lung
Hum. Pathol.
38
220-227
2007
Homo sapiens
Lu, S.C.
Regulation of glutathione synthesis
Mol. Aspects Med.
30
42-59
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Jackson, R.M.; Gupta, C.
Hypoxia and kinase activity regulate lung epithelial cell glutathione
Exp. Lung Res.
36
45-56
2010
Homo sapiens
Uchida, M.; Sugaya, M.; Kanamaru, T.; Hisatomi, H.
Alternative RNA splicing in expression of the glutathione synthetase gene in human cells
Mol. Biol. Rep.
37
2105-2109
2010
Homo sapiens (P48637), Homo sapiens
Dinescu, A.; Brown, T.R.; Barelier, S.; Cundari, T.R.; Anderson, M.E.
The role of the glycine triad in human glutathione synthetase
Biochem. Biophys. Res. Commun.
400
511-516
2010
Homo sapiens
Slavens, K.D.; Brown, T.R.; Barakat, K.A.; Cundari, T.R.; Anderson, M.E.
Valine 44 and valine 45 of human glutathione synthetase are key for subunit stability and negative cooperativity
Biochem. Biophys. Res. Commun.
410
597-601
2011
Homo sapiens
Brown, T.R.; Drummond, M.L.; Barelier, S.; Crutchfield, A.S.; Dinescu, A.; Slavens, K.D.; Cundari, T.R.; Anderson, M.E.
Aspartate 458 of human glutathione synthetase is important for cooperativity and active site structure
Biochem. Biophys. Res. Commun.
411
536-542
2011
Homo sapiens (P48637), Homo sapiens
EXTERNAL LINKS (specific for EC-Number 6.3.2.3)
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