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Information on EC 2.3.2.2 - gamma-glutamyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q680I5
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2.3.2.2 gamma-glutamyltransferaseIUBMB 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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- 2.3.2.2
- aminotransferase
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alt
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- albumin
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- bile
- biliary
- women
- creatinine
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- transaminase
- hepatocytes
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-
uric
-
c-reactive
- steatosis
- aminopeptidase
- jaundice
-
drinkers
-
hepatotoxicity
-
non-alcoholic
-
intrahepatic
- nafld
-
nephrotoxicity
-
ursodeoxycholic
-
waist
-
ultrasonography
- diethylnitrosamine
-
circumference
-
corpuscular
-
hepatocarcinogenesis
-
abuse
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hepatectomy
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- phenobarbital
-
preneoplastic
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-
homa-ir
-
abstinence
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-
n-acetyl-beta-d-glucosaminidase
- cholangitis
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cholangiopancreatography
- pharmacology
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elastography
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
a (5-L-glutamyl)-peptide
+
=
+
Synonyms
ggt, gamma-glutamyl transpeptidase, gamma-glutamyltransferase, gamma-glutamyltranspeptidase, gamma-gtp, gamma glutamyl transferase, glutamyl transpeptidase, gamma-glutamyl-transpeptidase, gammagt, blggt, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GGT2
alpha-glutamyl transpeptidase
-
-
-
-
gamma-glutamyl peptidyltransferase
-
-
-
-
gamma-glutamyl transpeptidase
-
-
-
-
gamma-GPT
-
-
-
-
gamma-GT
-
-
-
-
gamma-GTP
-
-
-
-
GGT1
GGT3
GGT4
glutamyl transpeptidase
-
-
-
-
glutamyltransferase, gamma-
-
-
-
-
L-gamma-glutamyl transpeptidase
-
-
-
-
L-gamma-glutamyltransferase
-
-
-
-
L-glutamyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminoacyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
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
9046-27-9
-
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
5-L-glutamyl 4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
in the standard GGT assay with gamma-glutamyl p-nitroanilide as substrate, GGT1 accounts for 80% to 99% of the activity in all tissues except seeds where GGT2 is 50% of the activity
-
-
?
5-L-glutamyl-4-methoxy-2-naphthylamide + glycylglycine
5-L-glutamyl-glycylglycine + 4-methoxy-2-naphthylamine
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
-
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
-
?
5-D-glutamyl-4-nitroanilide + acceptor
4-nitroaniline + 5-D-glutamyl-acceptor
-
-
?
5-L-glutamyl 4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
in the standard GGT assay with gamma-glutamyl p-nitroanilide as substrate, GGT1 accounts for 80% to 99% of the activity in all tissues except seeds where GGT2 is 50% of the activity
-
-
?
5-L-glutamyl-4-methoxy-2-naphthylamide + glycylglycine
5-L-glutamyl-glycylglycine + 4-methoxy-2-naphthylamine
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
-
-
-
?
5-L-glutamyl-7-amido-4-methylcoumarin + acceptor
7-amino-4-methylcoumarin + 5-L-glutamyl-acceptor
-
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
initial step of glutathione degradation
-
?
L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
L-Glu-4-nitroanilide is a suicide substrate
-
-
?
additional information
?
-
gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
-
-
?
additional information
?
-
-
gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
-
-
?
additional information
?
-
GGT3 catalyzes the obligate initial step in GSH conjugate metabolism, and has an important role in protecting plants from some xenobiotic chemicals
-
-
?
additional information
?
-
-
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
-
-
?
additional information
?
-
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
-
-
?
additional information
?
-
O65652
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
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
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
initial step of glutathione degradation
-
?
L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
L-Glu-4-nitroanilide is a suicide substrate
-
-
?
additional information
?
-
gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
-
-
?
additional information
?
-
-
gamma-glutamyl transpeptidase 4 catalyzes the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of Arabidopsis thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence
-
-
?
additional information
?
-
GGT3 catalyzes the obligate initial step in GSH conjugate metabolism, and has an important role in protecting plants from some xenobiotic chemicals
-
-
?
additional information
?
-
-
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
-
-
?
additional information
?
-
in the ggt1-1/ggt4-1/oxp1-1 triple mutant with no GGT activity in any organs except young siliques, the 5-oxoproline concentration in leaves is not different from that in oxp1-1 suggesting that GGTs are not major contributors to 5OP production in Arabidopsis
-
-
?
additional information
?
-
O65652
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
additional information
?
-
-
the rosettes of GGT1 knockouts show premature senescence after flowering
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
serine-borate
10 mM serine-borate inhibits enzyme activity
4-nitroaniline
strong, competitive against glutathione
serine-borate
10 mM serine-borate inhibits enzyme activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GGT3 is a major contributor to total GGT activity in roots, but a relatively minor contributor in other tissues
GGT1 accounts for nearly 100% of the activity in rosettes
GGT3 is a major contributor to total GGT activity in roots, but a relatively minor contributor in other tissues
additional information
GGT3 is a major contributor to total GGT activity in roots, but a relatively minor contributor in other tissues
GGT1 accounts for greater than 80% of the activity in stems and roots
GGT3 is a major contributor to total GGT activity in roots, but a relatively minor contributor in other tissues
GGT1 accounts for greater than 80% of the activity in stems and roots
GGT3 is a major contributor to total GGT activity in roots, but a relatively minor contributor in other tissues
additional information
O65652
GGT2 activity is below the detection limit of the assay in leaves and most other tissues of Arabidopsis
additional information
GGT2 activity is below the detection limit of the assay in leaves and most other tissues of Arabidopsis
additional information
GGT2 activity is below the detection limit of the assay in leaves and most other tissues of Arabidopsis
additional information
GGT2 activity is below the detection limit of the assay in leaves and most other tissues of Arabidopsis
additional information
-
GGT2 activity is below the detection limit of the assay in leaves and most other tissues of Arabidopsis
additional information
O65652
GGT4 activity, if present in the roots and stems, is near the limit of detection
additional information
GGT4 activity, if present in the roots and stems, is near the limit of detection
additional information
GGT4 activity, if present in the roots and stems, is near the limit of detection
additional information
GGT4 activity, if present in the roots and stems, is near the limit of detection
additional information
-
GGT4 activity, if present in the roots and stems, is near the limit of detection
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
recombinant enzyme is extracellular in transgenic tabacco plants
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GAGT2_ARATH
578
0
61600
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
amino acid sequence alignment, enzyme gene family
additional information
O65652
amino acid sequence alignment, enzyme gene family
additional information
amino acid sequence alignment, enzyme gene family
additional information
amino acid sequence alignment, enzyme gene family
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
additional information
O65652
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
additional information
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
additional information
construction of transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens transformation, functional extracellular overexpression of the Arabidopsis thaliana enzyme in leaves, transgenic and control plants show the same amount of glutathione degradation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression as His-tagged protein in Escherichia coli JM109, DNA sequence analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform GGT2 expression is enhanced in ggt1 knockout mutants, suggesting a compensatory effect to restore enzyme activity in the root apoplast. Supplementation with 0.1 mM glutathione results in the 4fold up-regulation of isoform GGT2 gene expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Storozhenko, S.; Belles-Boix, E.; Babiychuk, E.; Herouart, D.; Davey, M.W.; Slooten, L.; Van Montagu, M.; Inze, D.; Kushnir, S.
gamma-Glutamyl transpeptidase in transgenic tobacco plants. Cellular localization, processing, and biochemical properties
Plant Physiol.
128
1109-1119
2002
Arabidopsis thaliana, Arabidopsis thaliana (O65652), Arabidopsis thaliana (Q39078), Arabidopsis thaliana (Q9M0G0), Homo sapiens (P19440), Mus musculus (Q60928)
Grzam, A.; Martin, M.N.; Hell, R.; Meyer, A.J.
gamma-Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis
FEBS Lett.
581
3131-3138
2007
Arabidopsis thaliana (Q9M0G0), Arabidopsis thaliana
Ohkama-Ohtsu, N.; Zhao, P.; Xiang, C.; Oliver, D.J.
Glutathione conjugates in the vacuole are degraded by gamma-glutamyl transpeptidase GGT3 in Arabidopsis
Plant J.
49
878-888
2007
Arabidopsis thaliana (Q9M0G0)
Martin, M.N.; Saladores, P.H.; Lambert, E.; Hudson, A.O.; Leustek, T.
Localization of members of the gamma-glutamyl transpeptidase family identifies sites of glutathione and glutathione S-conjugate hydrolysis
Plant Physiol.
144
1715-1732
2007
Arabidopsis thaliana (O65652), Arabidopsis thaliana (Q680I5), Arabidopsis thaliana (Q9CAR5), Arabidopsis thaliana (Q9M0G0), Arabidopsis thaliana
Ohkama-Ohtsu, N.; Oikawa, A.; Zhao, P.; Xiang, C.; Saito, K.; Oliver, D.J.
A gamma-glutamyl transpeptidase-independent pathway of glutathione catabolism to glutamate via 5-oxoproline in Arabidopsis
Plant Physiol.
148
1603-1613
2008
Arabidopsis thaliana, Arabidopsis thaliana (Q9LR30)
Destro, T.; Prasad, D.; Martignago, D.; Bernet, I.L.; Trentin, A.R.; Renu, I.K.; Ferretti, M.; Masi, A.
Compensatory expression and substrate inducibility of gamma-glutamyl transferase GGT2 isoform in Arabidopsis thaliana
J. Exp. Bot.
62
805-814
2011
Arabidopsis thaliana, Arabidopsis thaliana (Q680I5), Arabidopsis thaliana (Q8VYW6), Arabidopsis thaliana (Q9M0G0)
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