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Information on EC 2.3.2.2 - gamma-glutamyltransferase and Organism(s) Bos taurus

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.2 gamma-glutamyltransferase
IUBMB Comments
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].
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Bos taurus
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ggt, gamma-glutamyl transpeptidase, gamma-glutamyltransferase, gamma-glutamyltranspeptidase, gamma-gtp, gamma glutamyl transferase, glutamyl transpeptidase, gamma-glutamyl-transpeptidase, gammagt, blggt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-glutamyl transpeptidase
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-
-
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gamma-glutamyl peptidyltransferase
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-
-
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gamma-glutamyl transpeptidase
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-
-
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gamma-glutamyltransferase
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gamma-glutamyltranspeptidase
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gamma-GPT
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-
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gamma-GT
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-
-
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gamma-GTP
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glutamyl transpeptidase
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glutamyltransferase, gamma-
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-
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L-gamma-glutamyl transpeptidase
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-
-
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L-gamma-glutamyltransferase
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-
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L-glutamyltransferase
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-
-
-
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
mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacyl group transfer
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-
-
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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
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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
-
-
-
-
?
1-menaphthylglutathione + glycylglycine
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenylglutathione + glycylglycine
?
show the reaction diagram
-
-
-
-
?
4-methylbiphenylylglutathione + glycylglycine
?
show the reaction diagram
-
-
-
-
?
4-nitrobenzylglutathione + glycylglycine
?
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + (S)-2-aminobutyrate
4-nitroaniline + N-[(1S)-1-carboxypropyl]-L-glutamine
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
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
show the reaction diagram
-
19% activity the rate of the reaction with glycylglycine, glycyl-tri- to hexapeptides can act as acceptors
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-
?
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 + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
show the reaction diagram
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-
-
-
?
5-L-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
show the reaction diagram
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-
-
-
?
5-L-glutamyl-4-nitroanilide + L-cysteine
4-nitroaniline + 5-L-glutamyl-L-cysteine
show the reaction diagram
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-
-
-
?
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
show the reaction diagram
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-
-
-
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
show the reaction diagram
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-
-
-
?
5-L-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
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-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-proline
4-nitroaniline + 5-L-glutamyl-L-proline
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
show the reaction diagram
-
-
-
-
?
9-methylanthracenylglutathione + glycylglycine
?
show the reaction diagram
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
show the reaction diagram
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-
-
-
?
L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
show the reaction diagram
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-
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?
L-glutamic acid 5-(3-carboxy-4-nitroanilide) + ?
?
show the reaction diagram
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-
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-
?
S-nitroso-glutathione + glycyl-glycine
S-nitroso-cysteinylglycine + gamma-L-glutamyl-glycyl-glycine
show the reaction diagram
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-
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-
?
additional information
?
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quantitation of gamma-glutamyl dipeptides by means of HPLC-MS/MS: quantification of gamma-Glu-Gly, gamma-Glu-Ala, gamma-Glu-Val, gamma-Glu-Thr, gamma-Glu-Asp, gamma-Glu-Lys, gamma-Glu-Glu, gamma-Glu-Trp, gamma-Glu-Leu, gamma-Glu-Ile, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-His, gamma-Glu-Phe, and gamma-Glu-Tyr in cheese samples after 13, 24, and 30 months of ripening (PC-13, PC-24, and PC-30), respectively, and in raw and heated cow milk, overview. gamma-Glu-Ala-[13C3] is used as the internal standard. High GGT activity to generate the gamma-GPs and preference for L-phenylalanine and L-methionine as acceptor amino acids are found in raw milk and milk samples heat-treated for 10 min up to a maximum of 65°C. In comparison, GGT activity and SIDL studies performed with inoculated Lactobacillus strains, including Lactobacillus harbinensis and Lactobacillus casei identified in Parmesan cheese (PC) by means of 16S rRNA gene sequencing, do not show any significant GGT activity and unequivocally demonstrate unpasteurized cow milk, rather than microorganisms, as a key factor in gamma-glutamyl dipeptide generation in Parmesan cheese
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NATURAL SUBSTRATE
NATURAL 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 + an amino acid
peptide + a 5-L-glutamyl amino acid
show the reaction diagram
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
show the reaction diagram
-
-
-
-
?
additional information
?
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quantitation of gamma-glutamyl dipeptides by means of HPLC-MS/MS: quantification of gamma-Glu-Gly, gamma-Glu-Ala, gamma-Glu-Val, gamma-Glu-Thr, gamma-Glu-Asp, gamma-Glu-Lys, gamma-Glu-Glu, gamma-Glu-Trp, gamma-Glu-Leu, gamma-Glu-Ile, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-His, gamma-Glu-Phe, and gamma-Glu-Tyr in cheese samples after 13, 24, and 30 months of ripening (PC-13, PC-24, and PC-30), respectively, and in raw and heated cow milk, overview. gamma-Glu-Ala-[13C3] is used as the internal standard. High GGT activity to generate the gamma-GPs and preference for L-phenylalanine and L-methionine as acceptor amino acids are found in raw milk and milk samples heat-treated for 10 min up to a maximum of 65°C. In comparison, GGT activity and SIDL studies performed with inoculated Lactobacillus strains, including Lactobacillus harbinensis and Lactobacillus casei identified in Parmesan cheese (PC) by means of 16S rRNA gene sequencing, do not show any significant GGT activity and unequivocally demonstrate unpasteurized cow milk, rather than microorganisms, as a key factor in gamma-glutamyl dipeptide generation in Parmesan cheese
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Acetazolamide Maleate
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Ca2+
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at 0.15 M
glutathione
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complete inhibition
Maleate
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Mg2+
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at 0.15 M
Na+
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0.1 M
additional information
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L-threonine is a poor gamma-glutamyl acceptor but facilitates the generation of gamma-Glu-Gln-[13C10], whereas L-phenylalanine is a good gamma-glutamyl acceptor but seemed to suppress the generation of gamma-Glu-Gln-[13C10], indicating an inhibitory effect as reported for glutathione
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Maleate
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stimulates hydrolase activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
1-menaphthylglutathione
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at pH 8.0 and 37°C
0.075
2,4-dinitrophenylglutathione
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at pH 8.0 and 37°C
0.23
4-methylbiphenylylglutathione
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at pH 8.0 and 37°C
0.3
4-nitrobenzylglutathione
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at pH 8.0 and 37°C
0.74
5-L-glutamyl-4-nitroanilide
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at pH 8.0 and 37°C
0.22
9-methylanthracenylglutathione
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at pH 8.0 and 37°C
0.687
glycyl-glycine
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pH 8.0, 37°C
10
glycylglycine
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0.8 - 1.3
L-Glu-4-nitroanilide
0.301
L-glutamic acid 5-(3-carboxy-4-nitroanilide)
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pH 8.0, 37°C
0.398
S-nitroso-glutathione
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pH 8.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
glutathione
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
407
-
purified enzyme
956
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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with acceptor glycylglycine
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 8.5
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about half-maximal activity at pH 7.3, maximal activity at pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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highest activity
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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very low activity
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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lactating, milk-membranes
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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gamma-glutamyl dipeptides (gamma-GPs) are responsible for the attractive Kokumi flavor of Parmesan cheese. They are synthesized by gamma-glutamyltransferase (GGT) from milk, most efficiently after 24 months of ripening (PC-24). GGT catalyzes the transfer of the gamma-glutamyl moiety of L-glutamine onto various acceptor amino acids released upon casein proteolysis. Microflora analysis in Parmesan cheese and GGT activity of Lactobacillus strains, overview. High GGT activity to generate the gamma-GPs and preference for L-phenylalanine and L-methionine as acceptor amino acids are found in raw milk and milk samples heat-treated for 10 min up to a maximum of 65°C. In comparison, GGT activity and SIDL studies performed with inoculated Lactobacillus strains, including Lactobacillus harbinensis and Lactobacillus casei identified in Parmesan cheese (PC) by means of 16S rRNA gene sequencing, do not show any significant GGT activity and unequivocally demonstrate unpasteurized cow milk, rather than microorganisms, as a key factor in gamma-glutamyl dipeptide generation in Parmesan cheese
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GGT6_BOVIN
490
0
49626
Swiss-Prot
other Location (Reliability: 3)
GGT7_BOVIN
662
1
70652
Swiss-Prot
other Location (Reliability: 1)
F1MYJ3_BOVIN
570
1
60884
TrEMBL
Secretory Pathway (Reliability: 1)
Q0V8S2_BOVIN
658
1
70250
TrEMBL
other Location (Reliability: 1)
G3N2D8_BOVIN
568
2
60874
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
gel filtration
110000
-
PAGE
25000
-
1 * 55000 + 1 * 25000, SDS-PAGE
25500
-
1 * 57000 + 1 * 25500, SDS-PAGE
27000
-
1 * 68000 + 1 * 27000, SDS-PAGE
28000
-
1 * 71000 + 1 * 28000, SDS-PAGE
55000
-
1 * 55000 + 1 * 25000, SDS-PAGE
57000
-
1 * 57000 + 1 * 25500, SDS-PAGE
68000
-
1 * 68000 + 1 * 27000, SDS-PAGE
71000
-
1 * 71000 + 1 * 28000, SDS-PAGE
80000
-
gel filtration
additional information
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amino acid composition
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial from ciliary body, solubilized with Emulphogene BC720
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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analytical method for the selective determination and speciation of S-nitrosoglutathione and its metabolite S-nitrosocysteinylglycine, based on liquid chromatography separation coupled to on-line enzymatic hydrolysis of S-nitrosoglutathione by commercial GGT. The limit of quantitation for S-nitrosoglutathione and S-nitrosocysteinylglycine in plasma ultrafiltrate is 5 nM, with a precision of 1-6% within the 5-1500 nM dynamic linear range. The method is applied to evaluate the recovery of exogenous S-nitrosoglutathione after addition of aliquots to human plasma samples presenting with different total GGT activities. By inhibiting GGT activity in a time-dependent manner, the recovery of S-nitrosoglutathione is inversely correlated with plasmatic levels of endogenous GGT
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hata, K.; Hayakawa, M.; Abiko, Y.; Takiguchi, H.
Purification and properties of gamma-glutamyl transpeptidase from bovine parotid gland
Int. J. Biochem.
13
681-692
1981
Bos taurus
Manually annotated by BRENDA team
Baumrucker, C.R.
Purification and identification of gamma-glutamyl transpeptidase of milk membranes
J. Dairy Sci.
63
49-54
1980
Bos taurus
Manually annotated by BRENDA team
Das, N.D.; Shichi, H.
gamma-Glutamyl transpeptidase of bovine ciliary body: purification and properties
Exp. Eye Res.
29
109-121
1979
Bos taurus
Manually annotated by BRENDA team
Yasumoto, K.; Iwami, K.; Fushiki, T.; Mitsuda, H.
Purification and enzymatic properties of gamma-glutamyltransferase from bovine colostrum
J. Biochem.
84
1227-1236
1978
Bos taurus
Manually annotated by BRENDA team
Furukawa, M.; Higashi, T.; Tateishi, N.; Ochi, K.; Sakamoto, Y.
Purification and properties of bovine liver gamma-glutamyltransferase
J. Biochem.
93
839-846
1983
Bos taurus
Manually annotated by BRENDA team
Angeli, V.; Tacito, A.; Paolicchi, A.; Barsacchi, R.; Franzini, M.; Baldassini, R.; Vecoli, C.; Pompella, A.; Bramanti, E.
A kinetic study of gamma-glutamyltransferase (GGT)-mediated S-nitrosoglutathione catabolism
Arch. Biochem. Biophys.
481
191-196
2009
Bos taurus
Manually annotated by BRENDA team
Bramanti, E.; Angeli, V.; Franzini, M.; Vecoli, C.; Baldassini, R.; Paolicchi, A.; Barsacchi, R.; Pompella, A.
Exogenous vs. endogenous gamma-glutamyltransferase activity: Implications for the specific determination of S-nitrosoglutathione in biological samples
Arch. Biochem. Biophys.
487
146-152
2009
Bos taurus
Manually annotated by BRENDA team
Agblor, A.A.; Josephy, P.D.
Donor substrate specificity of bovine kidney gamma-glutamyltransferase
Chem. Biol. Interact.
203
480-485
2013
Bos taurus
Manually annotated by BRENDA team
Hillmann, H.; Behr, J.; Ehrmann, M.; Vogel, R.; Hofmann, T.
Formation of Kokumi-enhancing gamma-glutamyl dipeptides in Parmesan cheese by means of gamma-glutamyltransferase activity and stable isotope double-labeling studies
J. Agric. Food Chem.
64
1784-1793
2016
Bos taurus, no activity in Lactobacillus casei, no activity in Lactobacillus harbinensis
Manually annotated by BRENDA team