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Information on EC 3.4.19.9 - folate gamma-glutamyl hydrolase and Organism(s) Homo sapiens and UniProt Accession Q92820

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.9 folate gamma-glutamyl hydrolase
IUBMB Comments
The enzyme, which occurs only in animals and plants, can be either endo- and/or exopeptidase. It acts on tetrahydropteroyl polyglutamates and their modified forms, as well as the polyglutamates of the folate breakdown product N-(4-aminobenzoyl)-L-glutamate (pABA-Glu). The initial cleavage may release either monoglutamate or poly-gamma-glutamate of two or more residues, depending on the specific enzyme. For example, GGH1 from the plant Arabidopsis thaliana cleaves pentaglutamates, mainly to di- and triglutamates, whereas GGH2 from the same organism yields mainly monoglutamates. The enzyme is lysosomal (and secreted) in animals and vacuolar in plants.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: Q92820
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
At1g78680, AtGGH1, AtGGH2, carboxypeptidase G, conjugase, EC 3.4.12.10, EC 3.4.22.12, FGPH, folate conjugase, folate hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxypeptidase G
-
-
-
-
conjugase
FGPH
-
-
-
-
folate conjugase
-
-
-
-
folic acid conjugase
-
-
-
-
folylpolyglutamate hydrolase
-
-
-
-
gamma-Glu-X carboxypeptidase
-
-
-
-
gamma-glutamyl hydrolase
hydrolase, gamma-glutamyl
-
-
-
-
low gamma-glutamyl hydrolase
283310
-
lysosomal gamma-glutamyl carboxypeptidase
-
-
-
-
poly(gamma-glutamic acid) endohydrolase
-
-
-
-
poly(glutamic acid) hydrolase II
-
-
-
-
polyglutamate hydrolase
-
-
-
-
pteroyl-poly-gamma-glutamate hydrolase
-
-
-
-
pteroylpoly-gamma-glutamyl hydrolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tetrahydropteroyl-(gamma-glutamyl)n + (n-1) H2O = 5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
tetrahydropteroyl-poly-gamma-glutamyl gamma-glutamyl hydrolase
The enzyme, which occurs only in animals and plants, can be either endo- and/or exopeptidase. It acts on tetrahydropteroyl polyglutamates and their modified forms, as well as the polyglutamates of the folate breakdown product N-(4-aminobenzoyl)-L-glutamate (pABA-Glu). The initial cleavage may release either monoglutamate or poly-gamma-glutamate of two or more residues, depending on the specific enzyme. For example, GGH1 from the plant Arabidopsis thaliana cleaves pentaglutamates, mainly to di- and triglutamates, whereas GGH2 from the same organism yields mainly monoglutamates. The enzyme is lysosomal (and secreted) in animals and vacuolar in plants.
CAS REGISTRY NUMBER
COMMENTARY hide
9074-87-7
not distinguishable from EC 3.4.17.11 in Chemical Abstracts
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,10-dideazatetrahydrofolate + H2O
?
show the reaction diagram
-
-
-
-
?
folate + H2O
pteroate + glutamate
show the reaction diagram
-
-
-
-
?
methotrexate + H2O
?
show the reaction diagram
-
-
-
-
?
methotrexate diglutamate + H2O
?
show the reaction diagram
methotrexate hexaglutamate + H2O
methotrexate pentaglutamate + methotrexate tetraglutamate + methotrexate triglutamate + methotrexate diglutamate + methotrexate monoglutamate
show the reaction diagram
-
-
-
?
methotrexate pentaglutamate + H2O
methotrexate tetraglutamate + methotrexate triglutamate + methotrexate diglutamate + methotrexate monoglutamate + L-glutamate
show the reaction diagram
-
-
-
?
methotrexate tetraglutamate + H2O
?
show the reaction diagram
-
-
-
-
?
methotrexate triglutamate + H2O
methotrexate monoglutamate + methotrexate diglutamate + glutamate
show the reaction diagram
-
-
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
show the reaction diagram
polyglutamylfolate + H2O
?
show the reaction diagram
pteroyldiglutamate + H2O
?
show the reaction diagram
-
-
-
-
?
pteroylglutamylhexaglutamate + H2O
short-chain pteroylglutamates
show the reaction diagram
-
-
after 60 min incubation, pteroylglutamate is the major product after 120 min, with quantitative recovery of free glutamate, enzyme is an exopeptidase which progressively hydrolyzes glutamyl units from pteroylpolyglutamate, leaving pteroylmonoglutamate as the folate form available for intestinal transport
?
pteroylheptaglutamate + H2O
?
show the reaction diagram
-
-
-
-
?
pteroylhexaglutamate + H2O
?
show the reaction diagram
-
-
-
-
?
pteroylpentaglutamate + H2O
?
show the reaction diagram
-
-
-
-
?
pteroylpolyglutamate + H2O
?
show the reaction diagram
pteroyltetraglutamate + H2O
?
show the reaction diagram
-
-
-
-
?
pteroyltriglutamate + H2O
?
show the reaction diagram
-
-
-
-
?
pteroyltriglutamate + H2O
pteroylglutamate + glutamate
show the reaction diagram
additional information
?
-
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
folate + H2O
pteroate + glutamate
show the reaction diagram
-
-
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
show the reaction diagram
-
-
-
-
?
pteroylpolyglutamate + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
slight activation
Fe2+
-
slight activation
Ni2+
-
slight activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-diazo-5-oxo-norleucine
-
-
acivicin
-
-
azaserine
-
-
gamma-diglutamate
-
-
iodoacetate
p-Aminobenzoate
-
0.1 mM: no inhibition, 30% inhibition at 1.0 mM
p-aminobenzoylglutamate
-
slight
p-hydroxymercuribenzoate
-
soluble intracellular enzyme is inhibited, membrane-bound brush-border enzyme not
Pterine
-
-
pteroyldiglutamate
-
hydrolysis of pteroyltriglutamate
Pteroylheptaglutamate
-
hydrolysis of pteroyltriglutamate
Salicylazosulfapyridine
-
-
substituted and reduced pteroylglutamate
-
0.1 mM: not, 30% inhibition at 1.0 mM
Zn2+
-
0.1 mM zinc acetate, weak
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-hydroxymercuribenzoate
-
slightly enhances activity
sulfhydryl compounds
-
activate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0214 - 0.049
methotrexate diglutamate
0.0006
pteroyldiglutamate
-
-
0.0006
Pteroylheptaglutamate
-
-
6
pteroyltetraglutamate
-
-
0.00055 - 0.0016
Pteroyltriglutamate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6
-
-
5.1
-
pteroyltetraglutamate
6 - 6.5
-
-
7.5
-
brush-border enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
-
about 45% of activity maximum at pH 4 and pH 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
about 25% of activity maximum at 30°C and 80°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
pulmonary, expression of gamma-glutamyl hydrolase correlates with poor prognosis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
vesicles
Manually annotated by BRENDA team
-
lysosome-like
Manually annotated by BRENDA team
-
intracellular
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
the association of -401C/T and +452C/T polymorphisms of gamma-glutamyl hydrolase and the risk of relapse to acute lymphoblastic leukemia is investigated. An association between the -401C/T polymorphism and the risk of relapse is found, patients with the -401T/T genotype have 10.83 more chance of a relapse of leukemia. No association is found between the +452C/T polymorphism and the risk of relapse
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
GGH_HUMAN
318
0
35964
Swiss-Prot
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35938
-
2 * 35938, recombinant His-tagged enzyme, dynamic light scattering, analytical ultracentrifugation, and sedimentation velocity measurement, nondissociating homodimer, homodimer formation is required for folding into the active conformation, overview
37000
-
x * 37000, SDS-PAGE
45000
-
soluble intracellular enzyme, gel filtration
71880
-
recombinant His-tagged enzyme, dynamic light scattering, analytical ultracentrifugation, and sedimentation velocity measurement
75000
-
human, gel filtration
83000
-
enzyme from jejunum
91000
-
membrane-bound enzyme, gel filtration
110000
115000
-
x * 145000 + x * 115000, SDS/urea PAGE
145000
-
x * 145000 + x * 115000, SDS/urea PAGE
700000
-
gel filtration
additional information
-
MW of detergent enzyme complexes: above 500000 Da
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, crystal structure at 1.6-A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C110A
-
inactive mutant enzyme
C124A
-
Km-value for methotrexate diglutamate is not significantly different from the Km-value of the wild-type enzyme. Specific activity is significantly lower than that of the wild-type enzyme, but the mutant protein has a higher amount of contaminating protein
C19A
-
Km-value for methotrexate diglutamate is not significantly different from the Km-value of the wild-type enzyme. Specific activity is significantly lower than that of the wild-type enzyme, but the mutant protein has a higher amount of contaminating protein
C290A
-
Km-value for methotrexate diglutamate is not significantly different from the Km-value of the wild-type enzyme
E222A
-
maximal velocity with methotrexate diglutamate is reduced 6fold relative to the wild-type enzyme
H171N
-
maximal velocity with methotrexate diglutamate is reduced 250fold relative to the wild-type enzyme
H220A
-
inactive mutant enzyme
H220N
-
site-directed mutagenesis, inactive mutant
T127I
-
distribution of the naturally occuring T127I polymorphism of the enzyme in a Japanese population, genotype distribution and allele frequency, Hardy-Weinberg equilibrium, comparison to Caucasians and in African-Americans populations, overview
additional information
-
the recombinant glycosylated enzyme forms very stable dimeric complexes with the recombinant His-tagged rat enzyme, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
stable at pH 6.5 and above, 90 min
647305
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
unstable at pH 4.5, protective effect of the substrate
50
-
jejunal enzyme stable, serum enzyme inactivated
65
-
up to, for at least 90 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol is required for stabilization
-
substrate protects
-
unaffected by dialysis against 1 mM EDTA
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, partially purified enzyme is stable for 3 months
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
baculovirus-expressed enzyme
-
recombinant enzyme expressed in Escherichia coli
-
recombinant N-terminally His-tagged enzyme from Hi5 insect cells, and non-tagged glycosylated enzyme from Hi5 insect cells by anion exchange chromatography
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
gene GGH, DNA and amino acid sequence determination and anaylsis, expression analysis, GGH promoter methylation is not a cause of GGH downregulation in CIMP+ colorectal cancer
-
expression the N-terminally His-tagged and non-tagged glycosylated enzyme in Hi5 insect cells
-
expression with a baculovirus/Sf9 insect cell expression system
-
gene GGH, DNA and amino acid sequence determination and analysis, genotyping, overview
-
GGH activity is directly related to GGH messenger RNA expression in acute lymphoblastic leukemia cells of patients with a wild-type germline GGH genotype, identification of two CpG islands, CpG1 and CpG2, in the region extending from the GGH promoter through the first exon and into intron 1, methylation of both CpG islands in the GGH promoter is associated with significantly reduced GGH mRNA expression and catalytic activity and with significantly higher accumulation of MTX polyglutamates in the cells, methylation of CpG1 is leukemia-cell specific and has a pronounced effect on GGH expression, whereas methylation of CpG2 is common in leukemia cells and normal leukocytes but does not significantly alter GGH expression, expression analysis, overview
-
overexpression in MCF7 breast cancer cells and HT1080 fibrosarcoma cells
-
wild-type and mutant enymes C19A, C110A, C124A and C290A are expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
reduced expression of GGH is a predictive factor of a reduced folate level after leucovorin administration in colorectal cancer
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
the relationships between the reduced folate levels in the colorectal cancer tissue after leucovorin administration and the gene-expression levels of folate-metabolizing enzymes and folate transporters is investigated. A multivariate logistic regression analysis reveals that low gamma-glutamyl hydrolase gene expression is a predictive factor for a high reduced folate level after leucovorin administration
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baugh, C.M.; Stevens, J.C.; Krumdieck, C.L.
Studies on gamma-glutamyl carboxypeptidase. I. The solid phase synthesis of analogs of polyglutamates of folic acid and their effects on human liver gamma-glutamyl carboxypeptidase
Biochim. Biophys. Acta
212
116-125
1970
Homo sapiens
Manually annotated by BRENDA team
Lakshmaiah, N.; Ramasastri, B.V.
Plasma folic acid conjugase
Methods Enzymol.
66
670-678
1980
Homo sapiens
Manually annotated by BRENDA team
Reisenauer, A.M.
Folate conjugase: two separate activities in human jejunum
Science
198
196-197
1977
Homo sapiens
Manually annotated by BRENDA team
Reisenauer, A.M.; Halsted, C.H.
Human jejunal brush border folate conjugase. Characteristics and inhibition by salicylazosulfapyridine
Biochim. Biophys. Acta
659
62-69
1981
Homo sapiens
Manually annotated by BRENDA team
Chandler, C.J.; Wang, T.T.Y.; Halsted, C.H.
Pteroylpolyglutamate hydrolase from human jejunal brush borders. Purification and characterization
J. Biol. Chem.
261
928-933
1986
Homo sapiens
Manually annotated by BRENDA team
Lavoie, A.; Tripp, E.; Hoffbrand, A.V.
Sephadex-gel filtration and heat stability of human jejunal and serum pteroylpolyglutamate hydrolase (folate conjugase). Evidence for two different forms
Biochem. Med.
13
1-6
1975
Homo sapiens
Manually annotated by BRENDA team
Wang, T.T.Y.; Chandler, C.J.; Halsted, C.H.
Intracellular pteroylpolyglutamate hydrolase from human jejunal mucosa. Isolation and characterization
J. Biol. Chem.
261
13551-13555
1986
Homo sapiens
Manually annotated by BRENDA team
Krungkrai, J.; Yuthavong, Y.; Webster, H.K.
High-performance liquid chromatographic assay for pteroylpolyglutamate hydrolase
J. Chromatogr.
417
47-56
1987
Homo sapiens
Manually annotated by BRENDA team
Gregory, J.F.3rd.; Ink, S.L.; Cerda, J.J.
Comparison of pteroylpolyglutamate hydrolase (folate conjugase) from porcine and human intestinal brush border membrane
Comp. Biochem. Physiol. B
88
1135-1141
1987
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Jaegerstad, M.; Olsson, I.
Pteroylpolyglutamate hydrolase of human granulocytes. I. Partial purification and kinetic studies
Scand. J. Clin. Lab. Invest.
39
343-349
1979
Homo sapiens
Manually annotated by BRENDA team
Chave, K.J.; Auger, I.E.; Galivan, J.; Ryan, T.J.
Molecular modeling and site-directed mutagenesis define the catalytic motif in human gamma -glutamyl hydrolase
J. Biol. Chem.
275
40365-40370
2000
Homo sapiens
Manually annotated by BRENDA team
Galivan, J.; Ryan, T.J.; Chave, K.; Rhee, M.; Yao, R.; Yin, D.
Glutamyl hydrolase: pharmacological role and enzymatic characterization
Pharmacol. Ther.
85
207-215
2000
Homo sapiens
Manually annotated by BRENDA team
Chave, K.J.; Galivan, J.; Ryan, T.J.
Site-directed mutagenesis establishes cysteine-110 as essential for enzyme activity in human gamma-glutamyl hydrolase
Biochem. J.
343
551-555
1999
Homo sapiens
Manually annotated by BRENDA team
Rhee, M.S.; Lindau-Shepard, B.; Chave, K.J.; Galivan, J.; Ryan, T.J.
Characterization of human cellular gamma-glutamyl hydrolase
Mol. Pharmacol.
53
1040-1046
1998
Homo sapiens
Manually annotated by BRENDA team
Li, H.; Ryan, T.J.; Chave, K.J.; Van Roey, P.
Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate
J. Biol. Chem.
277
24522-24529
2002
Homo sapiens
Manually annotated by BRENDA team
He, P.; Varticovski, L.; Bowman, E.D.; Fukuoka, J.; Welsh, J.A.; Miura, K.; Jen, J.; Gabrielson, E.; Brambilla, E.; Travis, W.D.; Harris, C.C.
Identification of carboxypeptidase E and gamma-glutamyl hydrolase as biomarkers for pulmonary neuroendocrine tumors by cDNA microarray
Hum. Pathol.
35
1196-1209
2004
Homo sapiens
Manually annotated by BRENDA team
Cheng, Q.; Cheng, C.; Crews, K.R.; Ribeiro, R.C.; Pui, C.H.; Relling, M.V.; Evans, W.E.
Epigenetic regulation of human gamma-glutamyl hydrolase activity in acute lymphoblastic leukemia cells
Am. J. Hum. Genet.
79
264-274
2006
Homo sapiens
Manually annotated by BRENDA team
Eisele, L.E.; Chave, K.J.; Lehning, A.C.; Ryan, T.J.
Characterization of human gamma-glutamyl hydrolase in solution demonstrates that the enzyme is a non-dissociating homodimer
Biochim. Biophys. Acta
1764
1479-1486
2006
Homo sapiens, Rattus norvegicus (Q62867)
Manually annotated by BRENDA team
Hayashi, H.; Fujimaki, C.; Inoue, K.; Suzuki, T.; Itoh, K.
Genetic polymorphism of C452T (T127I) in human gamma-glutamyl hydrolase in a Japanese population
Biol. Pharm. Bull.
30
839-841
2007
Homo sapiens
Manually annotated by BRENDA team
Kawakami, K.; Ooyama, A.; Ruszkiewicz, A.; Jin, M.; Watanabe, G.; Moore, J.; Oka, T.; Iacopetta, B.; Minamoto, T.
Low expression of gamma-glutamyl hydrolase mRNA in primary colorectal cancer with the CpG island methylator phenotype
Br. J. Cancer
98
1555-1561
2008
Homo sapiens (Q92820)
Manually annotated by BRENDA team
Schneider, E.; Ryan, T.J.
Gamma-glutamyl hydrolase and drug resistance
Clin. Chim. Acta
374
25-32
2006
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Pollard, C.; Nitz, M.; Baras, A.; Williams, P.; Moskaluk, C.; Theodorescu, D.
Genoproteomic mining of urothelial cancer suggests {gamma}-glutamyl hydrolase and diazepam-binding inhibitor as putative urinary markers of outcome after chemotherapy
Am. J. Pathol.
175
1824-1830
2009
Homo sapiens
Manually annotated by BRENDA team
Sadahiro, S.; Suzuki, T.; Maeda, Y.; Tanaka, A.; Ogoshi, K.; Kamijo, A.; Murayama, C.; Tsukioka, S.; Sakamoto, E.; Fukui, Y.; Oka, T.
Molecular determinants of folate levels after leucovorin administration in colorectal cancer
Cancer Chemother. Pharmacol.
65
735-742
2010
Homo sapiens, Homo sapiens (Q92820)
Manually annotated by BRENDA team
Smit, E.F.; Burgers, S.A.; Biesma, B.; Smit, H.J.; Eppinga, P.; Dingemans, A.M.; Joerger, M.; Schellens, J.H.; Vincent, A.; van Zandwijk, N.; Groen, H.J.
Randomized phase II and pharmacogenetic study of pemetrexed compared with pemetrexed plus carboplatin in pretreated patients with advanced non-small-cell lung cancer
J. Clin. Oncol.
27
2038-2045
2009
Homo sapiens
Manually annotated by BRENDA team
Organista-Nava, J.; Gomez-Gomez, Y.; Saavedra-Herrera, M.V.; Rivera-Ramirez, A.B.; Teran-Porcayo, M.A.; Alarcon-Romero, L.d.e.l..C.; Illades-Aguiar, B.; Leyva-Vazquez, M.A.
Polymorphisms of the gamma-glutamyl hydrolase gene and risk of relapse to acute lymphoblastic leukemia in Mexico
Leuk. Res.
34
728-732
2010
Homo sapiens
Manually annotated by BRENDA team
Kim, S.E.; Cole, P.D.; Cho, R.C.; Ly, A.; Ishiguro, L.; Sohn, K.J.; Croxford, R.; Kamen, B.A.; Kim, Y.I.
gamma-Glutamyl hydrolase modulation and folate influence chemosensitivity of cancer cells to 5-fluorouracil and methotrexate
Br. J. Cancer
109
2175-2188
2013
Homo sapiens
Manually annotated by BRENDA team
Kim, S.E.; Hinoue, T.; Kim, M.S.; Sohn, K.J.; Cho, R.C.; Cole, P.D.; Weisenberger, D.J.; Laird, P.W.; Kim, Y.I.
gamma-Glutamyl hydrolase modulation significantly influences global and gene-specific DNA methylation and gene expression in human colon and breast cancer cells
Genes Nutr.
10
444
2015
Homo sapiens
Manually annotated by BRENDA team
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