Information on EC 2.3.2.2 - gamma-glutamyltransferase and Organism(s) Homo sapiens

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Homo sapiens


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
2.3.2.2
-
RECOMMENDED NAME
GeneOntology No.
gamma-glutamyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
leukotriene biosynthesis
-
-
gamma-glutamyl cycle
-
-
hypoglycin biosynthesis
-
-
glutathione metabolism
-
-
Taurine and hypotaurine metabolism
-
-
Cyanoamino acid metabolism
-
-
Glutathione metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
(5-L-glutamyl)-peptide:amino-acid 5-glutamyltransferase
The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions [3-4].
CAS REGISTRY NUMBER
COMMENTARY hide
9046-27-9
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
cells overexpressing gamma-GT exhibit a low susceptibility to arsenic trioxide-induced apoptosis, associated with low reactive oxygen species induction and increased catalase activity
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
show the reaction diagram
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
show the reaction diagram
-
-
-
-
?
4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-GSH + glycylglycine
4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-(Cys-Gly) + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
4,4'-diphenylmethane diisocyanate linked GSH-GSH + glycylglycine
4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-GSH + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
5-L-glutamyl 3-carboxy-4-nitroanilide + glucana
5-amino-2-nitrobenzoic acid + N-(3-carboxy-4-nitrophenyl)-L-glutaminyl-L-glutamic acid
show the reaction diagram
-
-
-
ir
5-L-glutamyl 3-carboxy-4-nitronailide + glycylglycine
5-amino-2-nitrobenzoic acid + 5-L-glutamylglycylglycine
show the reaction diagram
5-L-glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine
3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-3-carboxy-4-nitroanilide + 5-L-glutamyl-3-carboxy-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-3-carboxy-4-nitroanilide + 3-carboxy-4-nitroaniline
show the reaction diagram
5-L-glutamyl-3-carboxy-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
show the reaction diagram
5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline
show the reaction diagram
-
autotranspeptidase
-
?
5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycyl-glycine
4-nitroaniline + 5-L-glutamyl-glycyl-glycine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycyl-L-proline
4-nitroaniline + 5-L-glutamyl-glycyl-L-proline
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
show the reaction diagram
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
show the reaction diagram
5-L-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
show the reaction diagram
-
hydrolase reaction
-
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
show the reaction diagram
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
show the reaction diagram
5-L-glutamyl-4-nitroanilide + L-leucyl-L-alanine
4-nitroaniline + 5-L-glutamyl-L-leucyl-L-alanine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-L-leucine + glycylglycine
L-Leu + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
?
7-(N-gamma-glutamylamino)-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + ?
show the reaction diagram
-
-
-
-
?
D-gamma-glutamyl-S-([4-[(4-aminophenyl)methyl]phenyl]carbamoyl)-L-cysteinylglycine + glycylglycine
S-([4-[(4-aminophenyl)methyl]phenyl]carbamoyl)-L-cysteinylglycine + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
gamma-glutamyl-S-[(6-[[([(2R)-2-amino-3-[(carboxymethyl)amino]-3-oxopropyl]sulfanyl)carbonyl]amino]hexyl)carbamoyl]cysteinylglycine + glycylglycine
(5R,20S)-5,20-diamino-4,8,17,21-tetraoxo-7,18-dithia-3,9,16,22-tetraazatetracosane-1,24-dioic acid + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
show the reaction diagram
-
-
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
show the reaction diagram
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
-
?
glutathione + Gly-Gly
L-cysteinylglycine + 5-L-glutamyl-Gly-Gly
show the reaction diagram
-
-
-
-
?
glutathione + H2O
L-cysteinylglycine + L-glutamate
show the reaction diagram
-
hydrolase reaction, concurrent to (auto-)transpeptidation
-
-
?
glutathione sulfonic acid + glycylglycine
?
show the reaction diagram
-
-
-
?
glutathionesulfonic acid + glycylglycine
?
show the reaction diagram
-
-
-
?
GSH + glycylglycine
L-Cys-Gly + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
?
GSSG + glycylglycine
L-Cys-Gly + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
?
hexane-1,6-diyldicarbamic acid linked GSH-GSH + glycylglycine
gamma-glutamyl-S-[(6-[[([(2R)-2-amino-3-[(carboxymethyl)amino]-3-oxopropyl]sulfanyl)carbonyl]amino]hexyl)carbamoyl]cysteinylglycine + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-S-[(6-aminohexyl)carbamoyl]-D-cysteinylglycine + glycylglycine
[[(2R)-2-amino-3-[[(6-aminohexyl)carbamoyl]sulfanyl]propanoyl]amino]acetic acid + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
show the reaction diagram
-
-
-
-
-
leukotriene C4 + glycylglycine
leukotriene D4 + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
?
S-(4-nitro-benzyl)glutathione + glycylglycine
?
show the reaction diagram
-
-
-
?
S-methylglutathione + glycylglycine
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
show the reaction diagram
-
-
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
show the reaction diagram
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
no effect
K+
-
no effect
Li+
-
no effect
Mg2+
-
no effect
Na+
-
no effect
additional information
-
no activation by Zn2+ and Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2,3,4-tetrahydroisoquinoline
-
the inhibitors can enhance cytostatic action of doxorubicin and cisplatin, which may permit clinicians to decrease their doses thereby alleviating side effects
2-amino 4-[4-chlorophenyl(methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 5.0/per mol * s
2-amino 4-[methyl(phenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 0.4/per mol * s
2-amino-4-[(4-methoxyphenyl)(methyl)phosphono]-butanoic acid
-
second-order rate constant for enzyme inactivation is 0.16/per mol * s
2-amino-4-[1-[N-(carboxymethyl)carbamoyl]propyl(phenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 75/per mol * s
2-amino-4-[4-cyanophenyl(methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 46/per mol * s
2-amino-4-[methyl(4-methylphenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 0.24/per mol * s
2-amino-4-[methyl(4-methylumbelliferyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 2400/per mol * s
2-amino-4-[methyl(4-nitrophenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 130/per mol * s
2-amino-4-[methyl(4-trifluoromethylphenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 12/per mol * s
2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 51/per mol * s
2-amino-4-[[4-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 0.33/per mol * s
4-chloro-N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
5-(L-alpha-glutamylamino)-2-nitrobenzoic acid
-
weak
-
5-(L-gamma-glutamylamino)-2-nitrobenzoic acid
-
enzyme from human tissues, not serum
5-Iodoacetamidofluorescein
-
inactivation, active site modification
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
methionine protects in vivo; transpeptidation, competitive to the glutamyl-donor, kinetics
6-diazo-5-oxo-L-norleucine
Acetazolamide Maleate
-
-
acivicin
brefeldin A
-
inhibition of recombinant mutant enzyme secretion into cell culture medium from Sf21 cells, accumulation in the cells
Bromocresol green
-
0.01 mM, 31% inhibition, noncompetitive
Co2+
-
weak
Cu2+
-
-
glutathione
-
-
glycylglycine
-
-
iodoacetamide
-
inhibition of transpeptidase reaction is more efficient than that of autotranspeptidase reaction
iodoacetate
-
weak
L-azaserine
L-methionine sulphoxide
-
-
-
L-Ser
-
in presence of borate, competitive
Maleate
-
-
N-(5-(4-methoxybenzyl)-1,3,4-thiadiazol-2-yl)benzenesulfonamide
-
-
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-chlorobenzenesulfonamide
-
-
N-ethylmaleimide
-
-
N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]-4-nitrobenzenesulfonamide
-
-
N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
N-[5-(4-methoxybenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
i.e. OU749. Competitive towards glycyclglycine, 150fold less toxic towards dividing cells than inhibitor acivicin. Inhibitory both to enzyme from 786-O cells and to human enzyme expressed in mouse fibroblast
NH4+
-
weak
p-hydroxymercuribenzoate
-
weak
serine-borate
competitive inhibitor which is 8fold more potent in inhibiting isoform GGT1 than in inhibiting isoform GGT5; competitive inhibitor which is 8fold more potent in inhibiting isoform GGT1 than in inhibiting isoform GGT5
Tris(hydroxymethyl)aminomethane
-
-
Urea
-
complete inactivation of wild-type and mutant at 6 M, low activity at 4 M
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Maleate
-
stimulates hydrolase reaction 3fold, inhibits transpeptidase reaction, with L-Glu as substrate
additional information
-
effect of amino acids on activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1 - 1.8
5-L-glutamyl-4-nitroanilide
0.0334
5-L-glutamyl-L-leucine
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0126
7-(N-gamma-glutamylamino)-4-methylcoumarin
-
25°C, pH 5.5
3.61
D-Glu-3-carboxy-4-nitroanilide
-
-
0.0346
glutathione sulfonic acid
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0751
glutathionesulfonic acid
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
2.9 - 16.9
glycylglycine
0.0105 - 0.0106
GSH
0.008 - 0.0426
GSSG
0.65 - 1.09
L-Glu-3-carboxy-4-nitroanilide
0.008 - 2.1
L-Glu-4-nitroanilide
0.0102 - 0.0108
leukotriene C4
0.0131 - 0.0148
S-(4-nitro-benzyl)glutathione
0.0099 - 0.0182
S-Methylglutathione
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1150
4-nitroanilide
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0287
4-chloro-N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
0.0102 - 0.0183
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
2.3
glycine
-
-
0.0759
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-chlorobenzenesulfonamide
-
-
0.0743
N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]-4-nitrobenzenesulfonamide
-
-
0.0433
N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
0.0738
N-[5-(4-methoxybenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
4.2 - 41.6
serine-borate
additional information
additional information
-
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine: Ki values in different tissues, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12
-
purified recombinant mutant H383A/H505A
16
-
purified enzyme
25.6
-
purified enzyme, normal and cirrhotic liver
47
-
purified recombinant mutant H505A
75.7
-
purified enzyme
81
-
purified enzyme
102.8
-
purified enzyme of cellular hepatic carcinoma
120
-
hepatoma
150
-
purified recombinant mutant H383A
200.4
-
purified enzyme
250
-
purified enzyme from liver
423
-
purified enzyme
440
-
purified recombinant wild-type enzyme
450
-
purified recombinant mutant enzyme
800
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
assay at
8.2 - 8.5
8.6
-
L-Glu-4-nitroanilide + glycylglycine
9.4
-
L-Glu-4-nitroanilide + L-Glu-4-nitroanilide
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
pH 6.5: about 50% of maximal activity, pH 9.0: about 90% of maximal activity
7 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
bronchial epithelial cell
Manually annotated by BRENDA team
-
cortex microvessels
Manually annotated by BRENDA team
-
WI-38 fetal
Manually annotated by BRENDA team
-
metastatic melanoma
Manually annotated by BRENDA team
-
GGT-overexpression in melanoma cells is associated with resistance to oxidative stress produced by prooxidant agents such as hydrogen peroxide and ascorbic acid
Manually annotated by BRENDA team
-
the enzyme is present in granules and released upon cell activation
Manually annotated by BRENDA team
-
ATCC CRL-1932, a GGT-positive renal cell adenocarcinoma line
Manually annotated by BRENDA team
-
whole body, fetal
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
-
recombinant wild-type in Sf21 cells
-
Manually annotated by BRENDA team
GGT1 is an extracellular enzyme that is anchored to the plasma membrane of cells
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
1 * 38000 + 1 * 14000, SDS-PAGE
20000
-
1 * 53000 + 1 * 20000, papain-solubilized, SDS-PAGE; 1 * 62000 + 1 * 20000, SDS-PAGE
21000
-
1 * 57000 + 1 * 21000, SDS-PAGE, presence of urea, 2-mercaptoethanol
24000
-
x * 43000-44000 + x * 24000, wild-type and mutant enzyme, SDS-PAGE
25000
1 * 64000 + 1 * 25000, isoform GGT5, SDS-PAGE
27000
-
1 * 61000 + 1 * 27000, SDS-PAGE
29000
-
1 * 64000 + 1 * 29000, SDS-PAGE
38000
-
1 * 38000 + 1 * 14000, SDS-PAGE
41500
-
x * 41500, heavy subunit of isoform GGT5, SDS-PAGE
47000
-
1 * 47000 + 1 * 22000, SDS-PAGE
53000
-
1 * 53000 + 1 * 20000, papain-solubilized, SDS-PAGE
54000
-
gel filtration
57000
-
1 * 57000 + 1 * 21000, SDS-PAGE, presence of urea, 2-mercaptoethanol
61000
-
1 * 61000 + 1 * 27000, SDS-PAGE
70000
-
there are four enzyme fractions in plasma of healthy subjects, named big-GGT, medium-GGT, small-GGT and free-GGT, with molecular weight corresponding to 2000, 1000, 250, and 70 kDa, respectively
71000
-
papain-solubilized, gel filtration
78000
-
seminal plasma, prostate, testis
80000
-
bile enzyme, gel filtration
82000
-
papain-solubilized enzyme, gel filtration
95000
-
1 * 150000 + 1 * 95000, SDS-PAGE
98000
-
Triton X-100-solubilized, PAGE
110000
150000
-
1 * 150000 + 1 * 95000, SDS-PAGE
160000
200000
-
Triton X-100 solubilized
210000
-
Triton X-100 solubilized
250000
300000
-
serum enzyme, gel filtration
500000
-
gel filtration without Triton X-100
1000000
-
there are four enzyme fractions in plasma of healthy subjects, named big-GGT, medium-GGT, small-GGT and free-GGT, with molecular weight corresponding to 2000, 1000, 250, and 70 kDa, respectively
2000000
-
there are four enzyme fractions in plasma of healthy subjects, named big-GGT, medium-GGT, small-GGT and free-GGT, with molecular weight corresponding to 2000, 1000, 250, and 70 kDa, respectively
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 77
-
in both the transpeptidation and hydrolysis reactions, wild type enzyme exhibits full activity up to 47°C. At temperatures greater than 62°C, the wild type enzyme is rendered completely inactive
56
-
30 min, 42% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PMSF stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C, freeze-dried, at least 3 months
-
-80°C, 9 months
-
2-8°C, 7 days
-
4°C, at least 5 days
-
4°C, t1/2: 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from normal and cirrhotic liver and 6 isoforms from serum of patients with cellular hepatic carcinoma
-
from seminal plasma, kidney, prostate, and testis
-
partial from bile
-
partial from liver
-
partial from liver; Triton X-100 solubilized liver enzyme is hydrophobic, papain-solubilized liver enzyme is hydrophilic
-
partial from pancreas and pancreatic carcinoma and pancreatic carcinoma cell line HPC-Y1
-
recombinant wild-type and mutants from Sf21 insect cells
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris and in HEK-293 cells
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expressed in Pichia pastoris; expressed in Pichia pastoris
expression in mouse fibroblast
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expression of recombinant wild-type and mutants in Spodoptera frugiperda Sf21 cells via baculovirus infection
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expression of wild-type and mutant lacking the putative signal sequence/anchor domain, amino acid 1-27, in Spodoptera frugiperda Sf21 cells via baculovirus infection
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transfection of human melanoma cell
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transfection of Me665/2 cell
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transfection of Me665/2/21 human melanoma cell, DU145 human prostatic carcinoma cell, and BEAS-2B human bronchial epithelial cell
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
tumor necrosis factor TNFalpha induces GGT promoter transactivation, mRNA and protein synthesis, as well as enzymatic activity. Remicade, a clinically used anti-TNFalpha antibody, small interfering RNA against p50 and p65 nuclear factor NF-kB isoforms, curcumin, a well characterized natural NF-kB inhibitor, as well as a dominant negative inhibitor IkBa, prevent GGT activation at various levels. Over-expression of receptor of TNFalpha-1, TNFR-associated factor-2 TRAF2, TNFR-1 associated death domain TRADD, dominant negative IkBa or NF-kB p65 further confirm GGT promoter activation via NF-kB.Mutation of the NF-kB site located at 110 additionally inhibits TNFalpha-induced promoter induction
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H383A
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site-directed mutagenesis of conserved His383 residue, 3fold reduced activity and 62% reduced Vmax, altered binding of acceptor
H383A/H505A
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site-directed mutagenesis, 37fold reduced activity
H505A
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site-directed mutagenesis, 10fold reduced activity
N120Q
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the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N230Q
-
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N266Q
-
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N297Q
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the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a slightly decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N344Q
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the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N511Q
-
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N95Q
-
the mutation results in an 8fold decrease in the cleavage efficiency of the propeptide
N95Q/N120Q/N230Q/N266Q/N297Q/N344Q/N511Q
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total N-glycosylation knock-out mutant
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine