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Information on EC 6.3.2.3 - glutathione synthase
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6.3.2.3 glutathione synthaseSpecify your search results
Word Map
- 6.3.2.3
- gamma-glutamylcysteine
- dismutase
- catalase
-
gamma-glutamyl
- sulfoximine
- s-transferase
-
5-oxoprolinuria
- cadmium
-
buthionine
- 5-oxoproline
- acidosis
-
hemolytic
- transpeptidase
- phytochelatins
- gamma-gcs
-
school-based
-
school
-
glutathione-related
-
atp-grasp
-
pyroglutamic
-
gsh-dependent
-
l-buthionine-s,r-sulfoximine
-
homoglutathione
-
bullied
- juncea
-
6.3.2.2
-
glutathione-deficient
- synthesis
- medicine
- biotechnology
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
Asuc_1947, bifunctional glutathione synthetase, bifunctional GSH synthetase, bifunctional L-glutathione synthetase, gamma -glutamate-cysteine ligase-glutathione synthetase, gamma-GCS, gamma-GCS-GS, gamma-glutamate-cysteine ligase/glutathione synthetase, gamma-glutamylcysteine synthetase-glutathione synthetase, GCL, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Asuc_1947
bifunctional glutathione synthetase
bifunctional GSH synthetase
bifunctional L-glutathione synthetase
gamma -glutamate-cysteine ligase-glutathione synthetase
-
bifunctional enzyme
gamma-GCS-GS
glutamate cysteine ligase
glutathione biosynthesis bifunctional protein GshAB
Glutathione synthase
Glutathione synthetase
Glutathione synthetase (tripeptide)
-
-
-
-
GS
GSH synthase
GSH synthetase
GSH-S
GSH2
gshAB
GSHase
-
-
-
-
gshB
GshF
GSHII
GSHS
GSS
Phytochelatin synthetase
-
-
-
-
Synthetase, glutathione
-
-
-
-
additional information
gamma-GCS-GS
-
bifunctional enzyme accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities
gamma-GCS-GS
-
bifunctional enzyme, with a glutathione synthetase at the C terminus
glutathione biosynthesis bifunctional protein GshAB
UniProt
glutathione biosynthesis bifunctional protein GshAB
UniProt
Glutathione synthase
-
-
-
-
Glutathione synthetase
-
-
-
-
Glutathione synthetase
bifunctional enzyme, also gamma-glutamylcysteine ligase activity, EC 6.3.2.2
GSH synthetase
-
-
-
-
GshF
-
bifunctional enzyme gamma -glutamate-cysteine ligase-glutathione synthetase
GSS
-
-
-
-
additional information
the enzyme belongs to the glutathione synthetase ATP-binding domain-like superfamily
additional information
enzyme belongs to the ATP-grasp enzyme superfamily
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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
determination of reaction and substrate binding mechanisms, large conformational changes in the catalytic cycle
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
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
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 SOURCE
PATHWAYS
BRENDA
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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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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
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-Ala
ADP + phosphate + gamma-L-Glu-L-Cys-beta-Ala
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-Ala
ADP + phosphate + gamma-L-Glu-L-Cys-L-Ala
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
-
-
?
ATP + L-gamma-Glu-Gly + Gly
ADP + phosphate + L-gamma-Glu-Gly-Gly
-
8% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
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
-
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-2-aminobutyrate + hydroxylamine
ADP + phosphate + gamma-(alpha-aminomethyl)Glu-2-aminobutyryl-Gly
-
-
-
-
?
ATP + gamma-Glu-2-aminobutyrate + hydroxylamine
ADP + phosphate + gamma-(alpha-aminomethyl)Glu-2-aminobutyryl-Gly
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
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-L-Cys + Gly
ADP + phosphate + glutathione
-
-
i.e. gamma-Glu-Cys-Gly
?
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
-
-
-
?
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-Ala
ADP + phosphate + gamma-Glu-L-Cys-beta-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
-
-
-
?
ATP + gamma-L-Glu-L-Cys + D-Ala
ADP + phosphate + gamma-Glu-L-Cys-D-Ala
-
-
-
?
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 + 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
-
-
-
?
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
-
-
-
?
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 + 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
-
-
-
?
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-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-Glu-L-Cys + L-Orn
ADP + phosphate + gamma-Glu-L-Cys-L-Orn
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Actinobacillus pleuropneumoniae ATCC 55618
-
-
-
?
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
-
-
-
?
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
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Streptococcus agalactiae serogroup 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
-
-
-
?
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
?
-
-
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 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-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
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
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
second step in the biosynthesis of glutahione
-
?
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
-
-
?
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
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
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Actinobacillus pleuropneumoniae ATCC 55618
-
-
-
?
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
-
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
-
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
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
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
-
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
-
-
-
-
?
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
the enzyme catalyzes the last step in glutathione biosynthesis
-
-
?
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
-
-
-
?
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 serogroup 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
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
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
?
-
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+
-
strict requirement for monovalent cation, maximal activity with K+
K+
-
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.
INHIBITOR
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.042
gamma-L-Glu-L-alpha-aminobutyrate
-
recombinant enzyme, pH 8.2, 37°C
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
0.18
ATP
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
0.26
ATP
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
0.299
ATP
pH 8.5, 40°C, recombinant His-tagged enzyme
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
7.5
gamma-Glu-L-Cys
-
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
0.25
gamma-L-glutamyl-L-cysteine
pH 7.8, 30°C, recombinant enzyme
1.13
gamma-L-glutamyl-L-cysteine
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
pH 8.5, 40°C, recombinant His-tagged enzyme
additional information
additional information
kinetics
-
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
-
Km-values of wild-type and mutant enzymes
-
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
-
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
-
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
2.94
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
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
3.13
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
3.25
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
6.08
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
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
-
loopless mutant with a 930fold decrease in turnover number
-
additional information
additional information
-
turnover number is fatally reduced in the P227V/G240V mutant
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29.6
ATP
pH 7.8, 30°C, recombinant enzyme, ATPase activity
23.8
ATP
pH 7.8, 28°C, recombinant enzyme, ATPase activity
16.9
ATP
pH 7.8, 25°C, recombinant enzyme, ATPase activity
13.4
ATP
pH 7.8, 20°C, recombinant enzyme, ATPase activity
7.1
ATP
pH 7.8, 15°C, recombinant enzyme, ATPase activity
5.1
ATP
pH 7.8, 10°C, recombinant enzyme, ATPase activity
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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
69.1
phosphate
25°C, pH 7.5, with gamma-Glu-L-Cys as varied substrate
69.1
phosphate
-
25°C, pH 7.5, with gamma-Glu-L-Cys as varied substrate
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.38
17.2
-
purified recombinant wild-type enzyme after complete proteoltic cleavage
21.9
-
purified recombinant enzyme mutant with eliminated cleavage site
additional information
0.38
simulated calculations, pH and temperature not specified in the publication
additional information
GshFAp has a glutathione synthetase catalytic activity with Vmax of 775 U/mg
additional information
GshFAp has a high gamma-GCS catalytic activity with Vmax of 1393 U/mg
additional information
-
assay development, activity under different reaction conditions in rat liver
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
7.3
7.5
8 - 8.5
8.2
8.5
8
recombinant cell surface-displayed enzyme in Saccharomyces cerevisiae