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Enzyme Nomenclature
Information on EC 6.3.2.3 - glutathione synthase
for references in articles please use BRENDA:EC6.3.2.3
Word Map on EC 6.3.2.3
- 6.3.2.3
- gamma-glutamylcysteine
- thiols
- peroxidase
- superoxide
-
gamma-glutamyl
- catalase
-
5-oxoprolinuria
-
buthionine
- sulfoximine
- cadmium
- 5-oxoproline
- acidosis
- anemia
-
hemolytic
- phytochelatins
- transpeptidase
-
pyroglutamic
-
atp-grasp
- gamma-ecs
- juncea
-
glutathione-deficient
-
glutathione-related
-
synthetase-deficient
-
school-based
-
6.3.2.2
-
homoglutathione
-
l-buthionine-s,r-sulfoximine
- synthesis
- biotechnology
- analysis
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
6.3.2.3
-
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RECOMMENDED NAME
GeneOntology No.
glutathione synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
the catalytic mechanism is proposed to proceed via phosphorylation of the dipeptide substrate to yield an acyl phosphate intermediate. This intermediate is subsequently attacked by glycine, followed by loss of inorganic phosphate, leading to glutathione formation
-
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
residues A534 and A535 are involved in substrate binding and determination of substrate specificity
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
substrate binding kinetics and mechanism, negative cooperativity of gamma-L-Glu-L-Cys
-
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
-
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
determination of reaction and substrate binding mechanisms, large conformational changes in the catalytic cycle
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
random ter-reactant reaction mechanism, overview
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
the reaction process involves the formation of an acyl phosphate on the cysteinyl moiety in L-gamma-glutamyl-L-cysteine, followed by the attack of the glycine and formation of an enzyme-product complex, which finally dissociates with the release of GSH, ADP and phosphate
-
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
the catalytic mechanism is proposed to proceed via phosphorylation of the dipeptide substrate to yield an acyl phosphate intermediate. This intermediate is subsequently attacked by glycine, followed by loss of inorganic phosphate, leading to glutathione formation
Escherichia coli B / ATCC 11303
-
-
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxamide formation
-
-
-
-
carboxylic acid-amide formation
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
gamma-L-glutamyl-L-cysteine:glycine ligase (ADP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
9023-62-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
B; wild-type and loopless mutant, in which the loop (Ile226-Arg241) is replaced with 3 Gly residues
-
-
JM109, wild-type, deletion mutant of the multifunctional loop and mutant with a nicked loop
-
-
wild-type and mutant enzymes: Cys294Ala, Cys409Ala, Cys422Ala and Cys294/Cys409/Cys422 to Ala294/Ala409/Ala422
-
-
mutant MN101 transformed with pYS41 containing the glutathione synthetase gene
-
-
bifucntional glutamate-cysteine ligase and glutathione synthetase
UniProt
bifucntional glutamate-cysteine ligase and glutathione synthetase
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Synechocystis glutathione synthase shares properties with other prokaryotic enzymes
evolution
homoglutathione synthetase, EC 6.3.2.23, has evolved from glutathione synthetase by a single gene duplication event
evolution
-
the enzyme is a member of the ATP-grasp superfamily of enzymes
evolution
Gsh2 belongs to the eu-GS superfamily; the enzyme encoded by GSH2 belongs to the eu-GC superfamily
evolution
-
the enzyme is a member of the ATP-grasp superfamily of enzymes
-
malfunction
a gene disruptant mutant strain without GSH2 gene grows poorly because GSH2 encoes the second step in GSH synthesis, the dipeptide intermediate, gamma-glutamylcysteine, can partially substitute for GSH
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
malfunction
-
a gene disruptant mutant strain without GSH2 gene grows poorly because GSH2 encoes the second step in GSH synthesis, the dipeptide intermediate, gamma-glutamylcysteine, can partially substitute for GSH
-
metabolism
A485L/T486P mutant shows a shift the substrate specificity increased affinity of GSH2 for Ser as a substrate, while affinity to Gly is preserved. This provides a new biosynthetic pathway for hydroxymethyl glutathione, which is known to be synthesized from glutathione and Ser in a reaction catalysed by carboxypeptidase Y
metabolism
-
the bifunctional enzyme gshF catalyzes both steps of glutathione biosynthesis in Streptococcus thermophilus
metabolism
the enzyme catalyzes the second step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine; the enzyme catalyzes the second step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine. GSH production occurs through two mechanisms: de novo synthesis and GSSG recycling. De novo synthesis occurs in a two-step reaction catalyzed by the two separate enzymes, glutamate cysteine ligase, EC 6.3.2.2, and glutathione synthetase
metabolism
-
the enzyme catalyzes the second step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine; the enzyme catalyzes the second step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine. GSH production occurs through two mechanisms: de novo synthesis and GSSG recycling. De novo synthesis occurs in a two-step reaction catalyzed by the two separate enzymes, glutamate cysteine ligase, EC 6.3.2.2, and glutathione synthetase
-
metabolism
-
the bifunctional enzyme gshF catalyzes both steps of glutathione biosynthesis in Streptococcus thermophilus
-
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
physiological function
-
the bifunctional GSH synthetase catalyzes two steps in GSH synthesis, which are usually catalyzed through L-glutamate L-cysteine ligase (gamma-GCS) and L-glutathione synthetase (GS)
physiological function
the enzyme is important in the biosynthesis of glutathione, the rate of GSH formation is limited by Gsh1 (EC 6.3.2.2), catalyzing the first step of the pathway; the enzyme is required for biosynthesis of glutathione. Glutathione (GSH) fulfills a variety of metabolic functions, participates in oxidative stress response, and defends against toxic actions of heavy metals and xenobiotics
physiological function
-
regulation of hGS plays a critical role in maintaining the cellular glutathione levels required to relieve oxidative stress
physiological function
-
the enzyme is important in the biosynthesis of glutathione, the rate of GSH formation is limited by Gsh1 (EC 6.3.2.2), catalyzing the first step of the pathway; the enzyme is required for biosynthesis of glutathione. Glutathione (GSH) fulfills a variety of metabolic functions, participates in oxidative stress response, and defends against toxic actions of heavy metals and xenobiotics
-
physiological function
-
the bifunctional GSH synthetase catalyzes two steps in GSH synthesis, which are usually catalyzed through L-glutamate L-cysteine ligase (gamma-GCS) and L-glutathione synthetase (GS)
-
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
structure comparisons and homology structure molecular modelling of the GSH2 wild-type 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
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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 + beta-aminoglutaryl-L-2-aminobutyrate + Gly
ADP + phosphate + beta-aminoglutaryl-L-2-aminobutyryl-Gly
ATP + DL-gamma-(beta-methyl)Glu-L-2-aminobutyrate + Gly
ADP + phosphate + DL-gamma-(beta-methyl)Glu-L-2-aminobutyryl-Gly
-
44% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
-
ATP + DL-gamma-(gamma-methyl)Glu-L-2-aminobutyrate + Gly
ADP + phosphate + DL-gamma-(gamma-methyl)Glu-L-2-aminobutyryl-Gly
-
16% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
-
ATP + gamma-(alpha-aminomethyl)Glu-2-aminobutyrate + Gly
ADP + phosphate + gamma-Glu-L-2-aminopentanoyl-Gly
-
-
-
-
-
ATP + gamma-Glu-2-aminobutyrate + hydroxylamine
ADP + phosphate + gamma-(alpha-aminomethyl)Glu-2-aminobutyryl-Gly
-
-
-
-
-
ATP + gamma-Glu-L-Cys + aminomethanesulfonic acid
ADP + phosphate + gamma-Glu-L-Cys-aminomethanesulfonic acid
Pigeon
-
-
-
-
-
ATP + gamma-Glu-L-Cys + aminooxyacetate
ADP + phosphate + gamma-Glu-Cys-aminoxyacetate
-
53% of the activity relative to Gly
-
-
-
ATP + gamma-Glu-L-Cys + N-hydroxyglycine
ADP + phosphate + gamma-Glu-Cys-N-hydroxyglycine
-
33% of the activity relative to Gly
-
-
-
ATP + gamma-L-Glu-aminobutanoate + Gly
ADP + phosphate + ophthalmic acid
-
-
-
-
?
ATP + gamma-L-Glu-L-alpha-aminobutyrate + Gly
ADP + phosphate + glutathione
-
-
-
r
ATP + gamma-L-Glu-L-Cys + 3-amino-1-propanol
ADP + phosphate + L-gamma-glutamyl-N-(3-hydroxypropyl)-L-cysteinamide
ATP + gamma-L-Glu-L-Cys + alpha-aminobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-alpha-aminobutyric acid
Q7X9G0, Q7X9G1
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-Ala
ADP + phosphate + gamma-L-Glu-L-Cys-beta-Ala
Q7X9G0, Q7X9G1
no activity with D-Ala
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-aminoisobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-beta-aminoisobutyric acid
ATP + gamma-L-Glu-L-Cys + beta-aminoisobutyric acid
ADP + phosphate + gamma-L-Glu-L-Cys-beta-aminoisobutyric acid
Q7X9G0, Q7X9G1
-
-
-
?
ATP + gamma-L-Glu-L-Cys + gamma-aminobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-gamma-aminobutyric acid
ATP + gamma-L-Glu-L-Cys + gamma-aminobutyric acid
ADP + phosphate + gamma-L-Glu-L-Cys-gamma-aminobutyric acid
Q7X9G0, Q7X9G1
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-2,3-diaminopropionic acid
ADP + phosphate + gamma-Glu-L-Cys-L-2,3-diaminopropionic acid
ATP + gamma-L-Glu-L-Cys + L-2,3-diaminopropionic acid
ADP + phosphate + gamma-L-Glu-L-Cys-L-2,3-diaminopropionic acid
Q7X9G0, Q7X9G1
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-Ala
ADP + phosphate + gamma-L-Glu-L-Cys-L-Ala
Q7X9G0, Q7X9G1
no activity with D-Ala
-
-
?
ATP + Glu-L-2-aminobutyrate + Gly
ADP + phosphate + gamma-Glu-L-Cys-Gly
-
16% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
-
ATP + L-gamma-(alpha-methyl)Glu-L-2-aminobutyrate + Gly
ADP + phosphate + L-gamma-(alpha-methyl)Glu-L-2-aminobutyryl-Gly
-
-
-
-
-
ATP + L-gamma-(N-methyl)Glu-L-2-aminobutyrate + Gly
ADP + phosphate + L-gamma-(N-methyl)Glu-L-2-aminobutyryl-Gly
-
52% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
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-
-
ATP + L-gamma-Glu-Gly + Gly
ADP + phosphate + L-gamma-Glu-Gly-Gly
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8% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
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-
-
ATP + L-gamma-Glu-L-2-aminopentanoic acid + Gly
ADP + phosphate + gamma-Glu-S-methylcysteinyl-Gly
-
9% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
-
ATP + L-gamma-Glu-L-Ala + Gly
ADP + phosphate + L-gamma-Glu-L-Ala-Gly
-
55% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
-
ATP + L-gamma-Glu-L-Cys + Gly
ADP + phosphate + L-gamma-Glu-L-Cys-Gly
-
102% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
-
ATP + L-gamma-Glu-L-Ser + Gly
ADP + phosphate + L-gamma-Glu-L-Ser-Gly
-
77% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
-
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 + N-acetyl-L-2-aminobutyrate + Gly
ADP + phosphate + N-acetyl-L-2-aminobutyrate-Gly
-
8% of the activity relative to L-gamma-glutamyl-L-2-aminobutyrate
-
-
-
ATP + N-acetyl-L-Cys + Gly
ADP + phosphate + N-acetyl-L-Cys-Gly
-
20% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
-
CTP + gamma-Glu-L-Cys + Gly
CDP + phosphate + glutathione
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4% of the activity relative to ATP
-
-
-
gamma-L-glutamyl-L-cysteine + glycine + ATP
ADP + phosphate + glutathione
-
-
-
?
glycine + ATP + gamma-L-glutamyl-L-cysteine
ADP + phosphate + glutathione
-
assay at pH 8.2
-
-
?
GTP + gamma-Glu-L-Cys + Gly
GDP + phosphate + glutathione
-
3% of the activity relative to ATP
-
-
-
ITP + gamma-Glu-L-Cys + Gly
IDP + phosphate + glutathione
-
6% of the activity relative to ATP
-
-
-
ATP + beta-aminoglutaryl-L-2-aminobutyrate + Gly
ADP + phosphate + beta-aminoglutaryl-L-2-aminobutyryl-Gly
-
-
-
-
-
ATP + beta-aminoglutaryl-L-2-aminobutyrate + Gly
ADP + phosphate + beta-aminoglutaryl-L-2-aminobutyryl-Gly
-
15% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
-
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
-
L-gamma-Glu-L-2-aminobutyrate
-
-
-
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
-
D-gamma-Glu-L-2-aminobutyrate
-
-
-
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
-
-
-
-
-
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
-
-
-
-
ATP + gamma-Glu-L-Cys + Ala
ADP + phosphate + gamma-Glu-Cys-Ala
-
beta-alanine
-
-
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
-
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
random ter-reactant mechanism, ADP is the last product released
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
i.e. gamma-Glu-Cys-Gly
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
i.e. gamma-Glu-Cys-Gly
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
i.e. gamma-Glu-Cys-Gly
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
Escherichia coli B / ATCC 11303
-
-
i.e. gamma-Glu-Cys-Gly
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
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-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
i.e. gamma-Glu-Cys-Gly
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
-
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-Glu-S-methylcysteine + Gly
ADP + phosphate + gamma-Glu-S-methylcysteinyl-Gly
-
-
-
-
-
ATP + gamma-Glu-S-methylcysteine + Gly
ADP + phosphate + gamma-Glu-S-methylcysteinyl-Gly
-
24% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
-
ATP + gamma-L-Glu-L-Cys + 3-amino-1-propanol
ADP + phosphate + L-gamma-glutamyl-N-(3-hydroxypropyl)-L-cysteinamide
-
-
-
?
ATP + gamma-L-Glu-L-Cys + 3-amino-1-propanol
ADP + phosphate + L-gamma-glutamyl-N-(3-hydroxypropyl)-L-cysteinamide
Q7X9G0, Q7X9G1
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-Ala
ADP + phosphate + gamma-Glu-L-Cys-beta-Ala
no activity with L-Ala or D-Ala
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-Ala
ADP + phosphate + gamma-Glu-L-Cys-beta-Ala
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-aminoisobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-beta-aminoisobutyric acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-aminoisobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-beta-aminoisobutyric acid
Q7X9G0, Q7X9G1
-
-
-
?
ATP + gamma-L-Glu-L-Cys + D-Ala
ADP + phosphate + gamma-Glu-L-Cys-D-Ala
-
-
-
?
ATP + gamma-L-Glu-L-Cys + D-Ser
ADP + phosphate + gamma-Glu-L-Cys-D-Ser
-
-
-
?
ATP + gamma-L-Glu-L-Cys + ethanolamine
ADP + phosphate + gamma-Glu-L-Cys-ethanolamine
-
-
-
?
ATP + gamma-L-Glu-L-Cys + ethanolamine
ADP + phosphate + gamma-Glu-L-Cys-ethanolamine
Q7X9G0, Q7X9G1
-
-
-
?
ATP + gamma-L-Glu-L-Cys + gamma-aminobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-gamma-aminobutyric acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + gamma-aminobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-gamma-aminobutyric acid
Q7X9G0, Q7X9G1
-
-
-
?
ATP + gamma-L-Glu-L-Cys + gamma-aminobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-gamma-aminobutyric acid
-
-
-
?
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
wild-type enzyme shows negative cooperativity
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
final step of glutathione biosynthesis
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
second step in the biosynthesis of glutahione
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
ApoE-deficient mice show reduced enzyme expression and activity, genetic regulation mechanism, overview
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
AF333982
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
in presence of dithiothreitol
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
wild-type enzyme shows negative cooperativity in binding of gamma-L-Glu-L-Cys
-
r
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
second step in the biosynthesis of glutahione
-
r
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
ir
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
final step in glutathione biosynthesis
-
ir
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
cells are not able to grow without glutathione, wild-type and all mutant enzyme forms can restore activity of the deficient mutant strain on minimal medium without glutathione
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
gene is regulated by stresses via the Atf1-Spc-1-Wis1 signal pathway
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
enzyme catalyzes the final step of glutathione biosynthesis
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-2,3-diaminopropionic acid
ADP + phosphate + gamma-Glu-L-Cys-L-2,3-diaminopropionic acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-2,3-diaminopropionic acid
ADP + phosphate + gamma-Glu-L-Cys-L-2,3-diaminopropionic acid
Q7X9G0, Q7X9G1
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-2,3-diaminopropionic acid
ADP + phosphate + gamma-Glu-L-Cys-L-2,3-diaminopropionic acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-Ala
ADP + phosphate + gamma-Glu-L-Cys-L-Ala
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-Orn
ADP + phosphate + gamma-Glu-L-Cys-L-Orn
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
D4N892
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Actinobacillus pleuropneumoniae ATCC 55618
D4N892
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
GSH homeostasis in plants is essential for cellular redox control and efficient responses to abiotic and biotic stress. Compartmentation of the GSH biosynthetic pathway is a unique feature of plants, restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development, overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
an optimally functioning two-step glutathione biosynthetic pathway is required in vivo for a robust defense against arsenite
-
-
?
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
-
-
?
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. Changes in GSH homeostasis occur in mice with liver-specific retinoid X receptor RXRalpha deletion
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
the enzyme catalyzes the last step in glutathione biosynthesis, loss of intracellular neuronal GSH is an important feature of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
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
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
the enzyme catalyzes the last step in glutathione biosynthesis
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Streptococcus agalactiae serotype V
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Streptococcus agalactiae serotype V ATCC BAA-611 / 2603 V/R
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
dATP + gamma-Glu-L-Cys + Gly
dADP + phosphate + glutathione
-
75% of the activity relative to ATP
-
-
-
UTP + gamma-Glu-L-Cys + Gly
UDP + phosphate + glutathione
-
10% of the activity relative to ATP
-
-
-
UTP + gamma-Glu-L-Cys + Gly
UDP + phosphate + glutathione
Escherichia coli B / ATCC 11303
-
10% of the activity relative to ATP
-
-
-
UTP + gamma-Glu-L-Cys + Gly
UDP + phosphate + glutathione
-
24% of the activity relative to ATP
-
-
-
additional information
?
-
-
the loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity
-
-
-
additional information
?
-
Escherichia coli B / ATCC 11303
-
the loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity
-
-
-
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
-
-
-
additional information
?
-
-
dysregulation of GSH synthesis 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
-
-
-
additional information
?
-
-
glutathione depletion is critical in cardiac dysfunction, antioxidant therapy shows positive effects on the redox state and in the disease, e.g. in metallothionein overexpressing transgenic mice or by application of buthionine sulfoximine, overview
-
-
-
additional information
?
-
-
the anti-oxidant response element promotes the expression of protective proteins including those required for glutathione synthesis, i.e. the xCT cystine antiporter, gamma-glutamylcysteine synthetase and glutathione synthase, overview
-
-
-
additional information
?
-
-
the consequences of GSH depletion include increased oxidative damage to proteins, lipids, and DNA and subsequent cytotoxic effects. GSH is also an important modulator of cellular copper homeostasis and altered Cu metabolism is central to the pathology of several neurodegenerative diseases. Both neurons and fibroblasts revealed increased expression and activation of p53 after depletion of GSH
-
-
-
additional information
?
-
-
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
-
additional information
?
-
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
-
additional information
?
-
-
assay method development based on [gamma32P]ATP hydrolysis coupled to the GSH synthesis, overview
-
-
-
additional information
?
-
assay method development based on [gamma32P]ATP hydrolysis coupled to the GSH synthesis, overview
-
-
-
additional information
?
-
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
-
additional information
?
-
assay method development based on [gamma32P]ATP hydrolysis coupled to the GSH synthesis, overview
-
-
-
additional information
?
-
-
the enzyme catalyzes ADP-ATP exchange at 0.62% of the rate of tripeptide synthesis
-
-
-
additional information
?
-
-
dysregulation of GSH synthesis 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
-
-
-
additional information
?
-
no activity with beta-alanine and L-serine by wild-type glutathione synthetase
-
-
-
additional information
?
-
-
the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3
-
-
-
additional information
?
-
-
the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
Q9FV26
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
Q9FV27, Q9FVA2
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
-
-
-
ir
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
-
final step of glutathione biosynthesis
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
P48637
second step in the biosynthesis of glutahione
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
Q94GA0
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
ApoE-deficient mice show reduced enzyme expression and activity, genetic regulation mechanism, overview
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
AF333982
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
second step in the biosynthesis of glutahione
-
r
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
Q08220
final step in glutathione biosynthesis
-
ir
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
gene is regulated by stresses via the Atf1-Spc-1-Wis1 signal pathway
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
enzyme catalyzes the final step of glutathione biosynthesis
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
D4N892
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Actinobacillus pleuropneumoniae ATCC 55618
D4N892
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
A6VQP8
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
P46416
GSH homeostasis in plants is essential for cellular redox control and efficient responses to abiotic and biotic stress. Compartmentation of the GSH biosynthetic pathway is a unique feature of plants, restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development, overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
an optimally functioning two-step glutathione biosynthetic pathway is required in vivo for a robust defense against arsenite
-
-
?
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
-
-
?
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. Changes in GSH homeostasis occur in mice with liver-specific retinoid X receptor RXRalpha deletion
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
the enzyme catalyzes the last step in glutathione biosynthesis, loss of intracellular neuronal GSH is an important feature of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Q3IFA2
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Q3IFA2
-
-
-
?
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
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
P46413
the enzyme catalyzes the last step in glutathione biosynthesis
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
A0A0U3DG08
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
A0A0U3DG08
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
P35669
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Streptococcus agalactiae serotype V
Q8DXM9
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Streptococcus agalactiae serotype V ATCC BAA-611 / 2603 V/R
Q8DXM9
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
D4N891
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
D4N891
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
P73493
-
-
-
?
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
-
-
-
additional information
?
-
-
dysregulation of GSH synthesis 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
-
-
-
additional information
?
-
-
glutathione depletion is critical in cardiac dysfunction, antioxidant therapy shows positive effects on the redox state and in the disease, e.g. in metallothionein overexpressing transgenic mice or by application of buthionine sulfoximine, overview
-
-
-
additional information
?
-
-
the anti-oxidant response element promotes the expression of protective proteins including those required for glutathione synthesis, i.e. the xCT cystine antiporter, gamma-glutamylcysteine synthetase and glutathione synthase, overview
-
-
-
additional information
?
-
-
the consequences of GSH depletion include increased oxidative damage to proteins, lipids, and DNA and subsequent cytotoxic effects. GSH is also an important modulator of cellular copper homeostasis and altered Cu metabolism is central to the pathology of several neurodegenerative diseases. Both neurons and fibroblasts revealed increased expression and activation of p53 after depletion of GSH
-
-
-
additional information
?
-
-
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
-
additional information
?
-
Q3IFA2
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
-
additional information
?
-
Q3IFA2
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
-
additional information
?
-
-
dysregulation of GSH synthesis 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
-
-
-
additional information
?
-
-
the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3
-
-
-
additional information
?
-
-
the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetate
-
anions that favor activity in decreasing order: acetate, HCOO-, Cl-, at 50 mM K+
Cd2+
-
transgenic plants overexpressing the enzyme from Escherichia coli show enhanced tolerance against cadmium, 3fold in the shoot
Cl-
-
anions that favor activity in decreasing order: acetate, HCOO-, Cl-, at 50 mM K+
Co2+
HCOO-
-
anions that favor activity in decreasing order: acetate, HCOO-, Cl-, at 50 mM K+
K+
Li+
Mg2+
Mn2+
NH4+
additional information
-
transgenic plants overexpressing the enzyme from Escherichia coli show enhanced salt tolerance
Co2+
-
divalent metal ion required, Mg2+ is most effective, Co2+ can replace Mg2+
K+
-
no requirement for exchange reaction; strict requirement for monovalent cation, maximal activity with K+
K+
-
maximal activation with 50 mM; strict requirement for monovalent cation, maximal activity with K+
Mg2+
a divalent cation is absolutely required for the activity, whereas monovalent cations are dispensable. Mg2+ is significantly more effective than Mn2+
Mn2+
a divalent cation is absolutely required for the activity, whereas monovalent cations are dispensable. Mg2+ is significantly more effective than Mn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine-5'-tetraphospho-5'-pyridoxal
-
when incubated with an adenosine-5'-polyphospho-5'-pyridoxal or pyridoxal phosphate in the presence of Mg2+ and then reduced with sodium borohydride, it is most rapidly inactivated by adenosine-5'-tetraphospho-5'-pyridoxal, addition of either ATP or gamma-glutamylcysteine protects from inactivation
-
c-jun
AF333982
negative regulation of enzyme expression by blocking the binding of AP-1 to the promotor
-
L-buthionine-(S,R)-sulfoximine
-
induction of enzyme expression at 0.01 mM
menadione
-
wild-type cells are not able to grow on menadione containing substrate, but the recombinant strain is able to survive at 0.1 mM menadione, induction of enzyme expression by superoxide generation
tert-butylhydroquinone
AF333982
regulatory role, activator protein 1 AP-1-mediated induction of enzyme expression, 35fold increase in activity in recombinant H4IIE cells, induction of c-jun formation, which is a negative regulatory protein blocking the binding of activator protein 1 to the promotor
5,5'-dithiobis(2-nitrobenzoate)
-
Cys289 is the only amino acid residue reactive with DTNB. Modification of Cys289 with DTNB results in complete loss of the catalytic activity
5,5'-dithiobis(2-nitrobenzoate)
-
inhibition of ADP-ATP exchange reaction, no effect on tripeptide synthesis
ADP
product inhibition, competitive versus ATP, noncompetitive versus gamma-L-glutamyl-L-cysteine and glycine
ATP
-
high concentrations inhibit the wild-type enzyme, while both nicked and loopless enzyme are not inhibited
buthionine sulfoximine
-
reduces the GSH level and the GSH/GSSG ratio without altering GSSG levels in hearts, livers, and kidneys
Cd2+
-
wild-type cells are not able to grow on cadmium chloride containing substrate, but the recombinant strain is able to survive at 1 mM cadmium chloride concentration, the wild-type can grow on 1 mM Cd2+ in presence of 20 mM GSH
glutathione
product inhibition, noncompetitive versus ATP, gamma-L-glutamyl-L-cysteine, and glycine
GSSG
the oxidised form of glutathione acts as an irreversible inhibitor of recombinant GshB
Hg2+
-
wild-type cells are not able to grow on mercuric chloride containing substrate, but the recombinant strain is able to survive at 0.01 mM mercuric chloride concentration, the wild-type can grow on 0.01 mM Hg2+ in presence of 20 mM GSH
NEM
-
inhibition of ADP-ATP exchange reaction, no effect on tripeptide synthesis
phosphate
product inhibition, noncompetitive versus ATP, gamma-L-glutamyl-L-cysteine, and glycine
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
-
additional information
-
no significant inhibition: amoxycillin, gentamycin, streptomycin, kanamycin, tetracycline, penicillin, artesunate, aablaquine and primaquine
-
additional information
-
enzyme expression in not affected by insulin and hydrocortisone treatment or by ethanol-feeding
-
additional information
-
no induction of enzyme expression by thioacetamide
-
additional information
insensitive to feedback inhibition caused by GSH even at 20 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
activator protein 1
AF333982
i.e. AP-1, mediates the induction of enzyme expression by tert-butylhydroquinone, binds to the enzyme promotor, antagonisted by c-jun, a dominant negative which is also produced in enhanced levels after treatment with tert-butylhydroquinone
-
buthionine sulfoximine
-
increase in enzyme expression in hepatocytes by 2.55fold after 18 h
monocrotaline
-
treatment of rats with monocrotaline, a pyrrolizidine alkaloid, increases the activity of GS
tert-butylhydroquinone
-
increase in enzyme expression in hepatocytes 1.7fold
tert-butylhydroquinone
AF333982
regulatory role, activator protein 1 AP-1-mediated induction of enzyme expression, 35fold increase in activity in recombinant H4IIE cells, induction of c-jun formation, which is a negative regulatory protein blocking the binding of activatot protein 1 to the promotor
Thioacetamide
-
increases the enzyme expression and activity in Chang cells by 50% at 6.66 mM
Thioacetamide
-
increases the enzyme expression and activity in hepatocyte cell culture and in liver 5fold in vivo
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
-
additional information
-
folate and vitamin E depletion leads to 18% increased enzyme expression and activity, mice mutants lacking apolipoprotein E show even higher activation rates of 31% on minimal diet compared to the wild-type on normal diet
-
additional information
-
(-)epicatechin upregulates the anti-oxidant response element, ARE, via an phosphatidylinositol 3-kinase-dependent pathway, ARE promotes the expression of protective proteins including those required for glutathione synthesis, i.e. the xCT cystine antiporter, gamma-glutamylcysteine synthetase and glutathione synthase, in cortical astrocytes, but not in neurons, overview, cyclic AMP response element and 3'-O-methyl-epicatechin play no significant role in enzyme upregulation
-
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 is required for basal expression of GS in the mouse
-
additional information
-
enzyme expression in not affected by insulin and hydrocortisone treatment or by ethanol-feeding, a partial hepatectomy lead to increase in enzyme expression 2.7fold after 12 h
-
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. Basal expression requires AP-1 and NFkappaB
-
additional information
tienilic acid induces the glutathione synthetase and all enzymes of the glutathione biosynthesis pathway, oxidative stress response, and phase II drug metabolism as do oxidative and/or electrophilic stresses, e.g. caused by tienilic acid, regulatory effects, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057
ATP
-
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.089
ATP
-
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.116
ATP
-
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.125
ATP
-
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.17
ATP
pH 7.8, 10°C, recombinant enzyme, ATPase activity
0.171
ATP
-
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.175
ATP
-
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.18
ATP
-
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.18
ATP
pH 7.8, 20°C, recombinant enzyme, ATPase activity; pH 7.8, 30°C, recombinant enzyme, ATPase activity
0.189
ATP
-
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.19
ATP
-
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.194
ATP
-
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.2 - 1
ATP
pH 7.8, 28°C, recombinant enzyme, ATPase activity
0.26
ATP
pH 7.8, 15°C, recombinant enzyme, ATPase activity; pH 7.8, 30°C, recombinant enzyme, with gamma-L-glutamyl-L-cysteine and glycine
0.28
ATP
pH 7.8, 25°C, recombinant enzyme, ATPase activity
0.346
ATP
-
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.37
ATP
-
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.695
ATP
-
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.785
ATP
-
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
4.9
ATP
-
mutant enzyme D448A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
13.4
ATP
-
mutant enzyme K489A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
0.035
gamma-Glu-L-Cys
-
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.039
gamma-Glu-L-Cys
-
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.129
gamma-Glu-L-Cys
-
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.143
gamma-Glu-L-Cys
-
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.146
gamma-Glu-L-Cys
-
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.166
gamma-Glu-L-Cys
-
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.271
gamma-Glu-L-Cys
-
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.273
gamma-Glu-L-Cys
-
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.425
gamma-Glu-L-Cys
-
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.954
gamma-Glu-L-Cys
-
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.94
gamma-Glu-L-Cys
-
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.34
gamma-Glu-L-Cys
-
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.6
gamma-Glu-L-Cys
-
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
5.9
gamma-Glu-L-Cys
-
wild type enzyme, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
7.03
gamma-Glu-L-Cys
-
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
7.5
gamma-Glu-L-Cys
-
mutant enzyme D448A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA; mutant enzyme K526A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
31
gamma-Glu-L-Cys
-
mutant enzyme K489A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
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
1.42
gamma-L-Glu-aminobutanoate
-
mutant V44A/V45A, pH 8.2, 37°C; wild-type, pH 8.2, 37°C
0.25
gamma-L-glutamyl-L-cysteine
pH 7.8, 30°C, recombinant enzyme
1.13
gamma-L-glutamyl-L-cysteine
D4N892
pH 8.5, 40°C, recombinant His-tagged enzyme
1.56
gamma-L-glutamyl-L-cysteine
pH 8.5, 40°C, recombinant His-tagged enzyme
1.18
Gly
-
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.51
Gly
-
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.67
Gly
-
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.69
Gly
-
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.16
Gly
-
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.25
Gly
-
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.4
Gly
-
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.41
Gly
-
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.45
Gly
-
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
4.04
Gly
-
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
4.17
Gly
-
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
6.3
Gly
-
wild type enzyme, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
6.59
Gly
-
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
7.57
Gly
-
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
11.8
Gly
-
mutant enzyme K526A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
16.1
Gly
-
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
23.8
Gly
-
mutant enzyme D448A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
28
Gly
-
mutant enzyme K489A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
1.3
glycine
D4N892
pH 8.5, 40°C, recombinant His-tagged enzyme
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
Km-values for Gly and gamma-Glu-Cys are sensitive to the mutation and drastically increased
-
additional information
additional information
-
loopless mutant with increased Km-values, especially for Gly
-
additional information
additional information
-
kinetics of cooperative substrate binding
-
additional information
additional information
-
kinetics, substrate and ligand binding, wild-type enzyme and mutants
-
additional information
additional information
-
the KM-value for gamma-L-Glu-L-Cys gives a distinctly nonlinear double-reciprocal plot
-
additional information
additional information
steady-state kinetics and kinetic mechanism, overview
-
additional information
additional information
-
steady-state kinetics and kinetic mechanism, overview
-
additional information
additional information
D4N892
kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.071
ATP
-
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.079
ATP
-
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.15
ATP
-
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.17
ATP
-
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.45
ATP
-
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.61
ATP
-
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.72
ATP
-
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.87
ATP
pH 7.8, 10°C, recombinant enzyme, ATPase activity
1.46
ATP
-
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.593
ATP
-
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.85
ATP
pH 7.8, 15°C, recombinant enzyme, ATPase activity
2.183
ATP
-
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.42
ATP
pH 7.8, 20°C, recombinant enzyme, ATPase activity
2.94
ATP
-
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase; mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3 - 6
ATP
-
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.183
ATP
-
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.3
ATP
-
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
4.72
ATP
pH 7.8, 25°C, recombinant enzyme, ATPase activity
4.99
ATP
pH 7.8, 28°C, recombinant enzyme, ATPase activity
5.083
ATP
-
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
5.32
ATP
pH 7.8, 30°C, recombinant enzyme, ATPase activity
5.7
ATP
-
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
12.1
ATP
-
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.011
gamma-Glu-L-Cys
-
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.059
gamma-Glu-L-Cys
-
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.077
gamma-Glu-L-Cys
-
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.158
gamma-Glu-L-Cys
-
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.383
gamma-Glu-L-Cys
-
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.842
gamma-Glu-L-Cys
-
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.973
gamma-Glu-L-Cys
-
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.485
gamma-Glu-L-Cys
-
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.51
gamma-Glu-L-Cys
-
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.13
gamma-Glu-L-Cys
-
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase; mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.25
gamma-Glu-L-Cys
-
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.3
gamma-Glu-L-Cys
-
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.517
gamma-Glu-L-Cys
-
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.817
gamma-Glu-L-Cys
-
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
5.317
gamma-Glu-L-Cys
-
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
6.08
gamma-Glu-L-Cys
-
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase; mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
12.2
gamma-Glu-L-Cys
-
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.062
Gly
-
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.08
Gly
-
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.157
Gly
-
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.22
Gly
-
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.29
Gly
-
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.37
Gly
-
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.03
Gly
-
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.08
Gly
-
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.33
Gly
-
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.467
Gly
-
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.583
Gly
-
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.94
Gly
-
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3 - 6
Gly
-
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.3
Gly
-
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
5.183
Gly
-
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
7.2
Gly
-
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
12.6
Gly
-
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
additional information
additional information
-
turnover-numbers of wild-type and mutant enzymes
-
additional information
additional information
-
turnover number is fatally reduced in the P227V/G240V mutant
-
additional information
additional information
-
loopless mutant with a 930fold decrease in turnover number
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.1
ATP
pH 7.8, 10°C, recombinant enzyme, ATPase activity
7.1
ATP
pH 7.8, 15°C, recombinant enzyme, ATPase activity
13.4
ATP
pH 7.8, 20°C, recombinant enzyme, ATPase activity
16.9
ATP
pH 7.8, 25°C, recombinant enzyme, ATPase activity
23.8
ATP
pH 7.8, 28°C, recombinant enzyme, ATPase activity
29.6
ATP
pH 7.8, 30°C, recombinant enzyme, ATPase activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16.6
glutathione
-
25°C, pH 7.5, with gamma-Glu-L-Cys as varied substrate
38.6