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(4,4-difluoro)glutamyl-gamma-glutamate + H2O
(4,4-difluoro)glutamate + glutamate
-
the fluorine substitution results in a significant decrease in rates of hydrolysis under steady-state conditions due primarily to a 15fold increase in Km compared to the unsubstituted substrate
-
-
?
(poly-gamma-glutamate)n + H2O
(poly-gamma-glutamate)n-1 + glutamate
-
-
-
-
?
(poly-gamma-L-glutamate)n + H2O
oligo-gamma-L-glutamate
-
-
-
-
?
2,4-diamino-10-methyl-pteroylglutamyl-gamma-glutamate + H2O
2,4-diamino-10-methyl-pteroate + glutamate + gamma-glutamylglutamate
4-aminobenzoyl-(4,4-difluoro)glutamyl-gamma-glutamate + H2O
4-aminobenzoyl-(4,4-difluoro)glutamate + glutamate
-
the fluorine substitution results in a significant decrease in rates of hydrolysis under steady-state conditions due primarily to a 15fold increase in Km compared to the unsubstituted substrate
-
-
?
4-aminobenzoyl-gamma-Glu + H2O
4-aminobenzoate + Glu
-
-
-
-
?
4-aminobenzoyl-gamma-Glu-gamma-Glu-Tyr + H2O
?
-
-
-
-
?
4-aminobenzoyl-penta-gamma-glutamate + H2O
4-aminobenzoylglutamate + tetra-gamma-glutamate
-
-
subsequently degraded to glutamic acid
?
4-aminobenzoyltriglutamate + H2O
?
-
at 13% the rate of pteroyltriglutamate hydrolysis
-
-
?
4-hydroxy-2-nonenal-glutathione conjugate + H2O
4-hydroxy-2-nonenal-[Cys-Gly] conjugate + L-glutamate
-
-
-
-
?
5,10-dideazatetrahydrofolate + H2O
?
-
-
-
-
?
5,10-methenyltetrahydrofolate glutamate + H2O
5,10-methenyltetrahydrofolate + L-glutamate
-
-
-
?
5,10-methenyltetrahydrofolate heptaglutamate + 7 H2O
5,10-methenyltetrahydrofolate + 7 L-glutamate
-
-
-
?
5,10-methenyltetrahydrofolate hexaglutamate + 6 H2O
5,10-methenyltetrahydrofolate + 6 L-glutamate
-
-
-
?
5-formyltetrahydrofolate glutamate + H2O
5-formyltetrahydrofolate + L-glutamate
-
-
-
?
5-formyltetrahydrofolate heptaglutamate + 7 H2O
5-formyltetrahydrofolate + 7 L-glutamate
-
-
-
?
5-formyltetrahydrofolate hexaglutamate + 6 H2O
5-formyltetrahydrofolate + 6 L-glutamate
-
-
-
?
5-formyltetrahydrofolate triglutamate + H2O
?
5-L-glutamyl-4-nitroanilide + H2O
L-glutamic acid + 4-nitroaniline
-
-
-
-
?
5-methyltetrahydrofolate glutamate + H2O
5-methyltetrahydrofolate + L-glutamate
-
-
-
?
5-methyltetrahydrofolate heptaglutamate + 7 H2O
5-methyltetrahydrofolate + 7 L-glutamate
-
-
-
?
5-methyltetrahydrofolate hexaglutamate + 6 H2O
5-methyltetrahydrofolate + 6 L-glutamate
-
-
-
?
di-gamma-L-glutamate + H2O
L-glutamate
-
-
-
-
?
folate + H2O
pteroate + glutamate
-
-
-
-
?
folic acid pentaglutamate + H2O
?
PteGlu5
-
-
?
glutamyl-gamma-glutamate + H2O
glutamate
-
-
-
-
?
L-glutamic acid gamma-(4-nitroanilide) + H2O
L-glutamic acid + 4-nitroaniline
-
-
-
-
?
methotrexate + H2O
?
-
-
-
-
?
methotrexate diglutamate + H2O
?
methotrexate hexaglutamate + H2O
methotrexate pentaglutamate + methotrexate tetraglutamate + methotrexate triglutamate + methotrexate diglutamate + methotrexate monoglutamate
-
-
-
?
methotrexate penta-gamma-glutamate + H2O
methotrexate-gamma-glutamate + tetra-gamma-glutamate
-
-
subsequently degraded to glutamic acid
?
methotrexate pentaglutamate + H2O
methotrexate glutamate + tetra-gamma-L-glutamate
-
-
-
?
methotrexate pentaglutamate + H2O
methotrexate tetraglutamate + methotrexate triglutamate + methotrexate diglutamate + methotrexate monoglutamate + L-glutamate
-
-
-
?
methotrexate polyglutamate + H2O
?
-
-
-
-
?
methotrexate tetraglutamate + H2O
?
-
-
-
-
?
methotrexate triglutamate + H2O
methotrexate monoglutamate + methotrexate diglutamate + glutamate
-
-
-
-
?
N5-methyltetrahydropteroyltetraglutamate + H2O
?
-
cleaves the terminal gamma-glutamyl residues, finally releasing a monoglutamyl end-product
-
-
?
oligo-gamma-L-glutamate + H2O
L-glutamate
-
-
-
-
?
p-aminobenzoyl-penta-gamma-glutamate + H2O
?
p-aminobenzoylpentaglutamate + H2O
?
pABAGlu5
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
polyglutamylfolate + H2O
?
pteroyl-penta-gamma-glutamate + H2O
?
pteroyldiglutamate + H2O
?
-
-
-
-
?
pteroylglutamylhexaglutamate + H2O
short-chain pteroylglutamates
-
-
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
?
pteroylhexaglutamate + H2O
?
-
-
-
-
?
pteroylpentaglutamate + H2O
?
pteroylpolyglutamate + H2O
?
pteroyltetraglutamate + H2O
?
-
-
-
-
?
pteroyltriglutamate + H2O
?
pteroyltriglutamate + H2O
pteroylglutamate + glutamate
tetra-gamma-L-glutamate + H2O
L-glutamate
-
-
-
-
?
tri-gamma-L-glutamate + H2O
L-glutamate
-
-
-
-
?
additional information
?
-
2,4-diamino-10-methyl-pteroylglutamyl-gamma-glutamate + H2O
2,4-diamino-10-methyl-pteroate + glutamate + gamma-glutamylglutamate
-
-
bile enzyme at a ratio of 5:95 and plasma enzyme at a ratio of 23:77
?
2,4-diamino-10-methyl-pteroylglutamyl-gamma-glutamate + H2O
2,4-diamino-10-methyl-pteroate + glutamate + gamma-glutamylglutamate
-
-
bile enzyme at a ratio of 5:95 and plasma enzyme at a ratio of 23:77
?
5-formyltetrahydrofolate triglutamate + H2O
?
-
-
-
?
5-formyltetrahydrofolate triglutamate + H2O
?
-
-
-
?
glutathione + H2O
?
-
-
-
-
?
glutathione + H2O
?
-
enzyme hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress
-
-
?
glutathione + H2O
?
-
-
-
-
?
glutathione + H2O
?
-
enzyme hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress
-
-
?
methotrexate diglutamate + H2O
?
-
-
-
-
?
methotrexate diglutamate + H2O
?
-
poor substrate
-
-
?
p-aminobenzoyl-penta-gamma-glutamate + H2O
?
AtGGH1 cleaves pentaglutamates mainly to di- and triglutamates
-
-
?
p-aminobenzoyl-penta-gamma-glutamate + H2O
?
AtGGH2 cleaves pentaglutamates mainly to monoglutamates
-
-
?
poly-Glu + H2O
?
Micromonospora melanosporea
-
-
Glu-Glu + oligomers of Glu
?
poly-Glu + H2O
?
-
enzyme is specific for poly(gamma-glutamic) acid, but not for other gamma-glutamyl peptides or amides
endo-type specificity, 38% of the original poly-Glu with an average MW of 500000 is converted to smaller peptides, and then depolymerized to a mixture of gamma-oligopeptides which consist of only L-glutamic acid, L-glutamic acid monomer is negligible in the reaction mixture, the remaining 62% of poly(gamma-glutamic acid) are resistant to the enzyme action
?
poly-Glu + H2O
?
-
enzyme is specific for poly(gamma-glutamic) acid, but not for other gamma-glutamyl peptides or amides
endo-type specificity, 38% of the original poly-Glu with an average MW of 500000 is converted to smaller peptides, and then depolymerized to a mixture of gamma-oligopeptides which consist of only L-glutamic acid, L-glutamic acid monomer is negligible in the reaction mixture, the remaining 62% of poly(gamma-glutamic acid) are resistant to the enzyme action
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
-
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
removal of the poly-gamma-glutamate chains
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
-
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
-
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
gamma-glutamyl hydrolase, not glutamate carboxypeptidase II, hydrolyzes dietary folate in rat small intestine
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
removal of the poly-gamma-glutamate chains
-
-
?
polyglutamylfolate + H2O
?
-
bond cleavage occurs with equal facility at internal points of the peptide chain
-
-
?
polyglutamylfolate + H2O
?
-
longer chain gamma-glutamyl peptides are preferentially attacked by the enzyme
-
-
?
polyglutamylfolate + H2O
?
-
peptide bond cleavage occurs only at gamma-glutamyl bonds and the presence of a COOH-terminal gamma bond is essential for enzyme action
-
-
?
polyglutamylfolate + H2O
?
-
the cleavage of diglutamyl peptides is extremely slow
-
-
?
polyglutamylfolate + H2O
?
-
the cleavage of gamma bonds is independent of the NH2-terminal pteroyl moiety
-
-
?
polyglutamylfolate + H2O
?
-
endopeptidase-like mode of action
-
-
?
polyglutamylfolate + H2O
?
-
the ability of the gamma polyglutamate and the inability of the alpha polyglutamate to serve as substrate confirm the requirement for a terminal gamma peptide bond
-
-
?
polyglutamylfolate + H2O
?
-
sequential hydrolysis of glutamates with the dissociation of substrate from enzymic surface following cleavage of each glutamate seems likely
-
-
?
polyglutamylfolate + H2O
?
-
longer chain gamma-glutamyl peptides are preferentially attacked by the enzyme
-
-
?
polyglutamylfolate + H2O
?
-
specificity towards analogs of pteroylglutamyl-gamma-glutamyl-gamma-glutamic acid
-
-
?
polyglutamylfolate + H2O
?
-
analogs of the general structure pteroylglutamyl-gamma-glutamyl-gamma-R serve as substrates, low degree of specificity with regard to the nature of the-R group
-
-
?
polyglutamylfolate + H2O
?
-
enzyme from mouse kidney shows mixed endo- and exopeptidase activity, the enzyme from all other normal tissues and tumor cells is consistent with endopeptidase activity
-
-
?
polyglutamylfolate + H2O
?
-
-
-
-
?
polyglutamylfolate + H2O
?
-
endopeptidase-like mode of action
-
-
?
polyglutamylfolate + H2O
?
-
endo/random hydrolysis of gamma-glutamyl peptide bonds of pteroylpolyglutamate substrates yielding folic acid as the terminal product
-
-
?
pteroyl-penta-gamma-glutamate + H2O
?
AtGGH1 cleaves pentaglutamates mainly to di- and triglutamates
-
-
?
pteroyl-penta-gamma-glutamate + H2O
?
AtGGH2 cleaves pentaglutamates mainly monoglutamates
-
-
?
pteroylheptaglutamate + H2O
?
-
-
pteroyldiglutamate + gamma-Glu5
?
pteroylheptaglutamate + H2O
?
-
-
-
-
?
pteroylheptaglutamate + H2O
?
-
-
pteroylmonoglutamate + hexaglutamyl peptide
?
pteroylpentaglutamate + H2O
?
-
-
-
-
?
pteroylpentaglutamate + H2O
?
-
-
-
-
?
pteroylpentaglutamate + H2O
?
-
-
-
-
?
pteroylpentaglutamate + H2O
?
-
-
-
-
?
pteroylpolyglutamate + H2O
?
-
the enzyme is responsible for the intracellular cleavage of poly-gamma-glutamates
-
-
?
pteroylpolyglutamate + H2O
?
-
the enzyme is suggested to be involved in the destruction of microorganisms in granulocytes during phagocytosis
-
-
?
pteroylpolyglutamate + H2O
?
-
central enzyme in folyl and antifolylpoly-gamma-glutamate metabolism
-
-
?
pteroylpolyglutamate + H2O
?
-
key enzyme in the maintenance of cellular folylpolyglutamate concentration
-
-
?
pteroylpolyglutamate + H2O
?
-
central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism
-
-
?
pteroylpolyglutamate + H2O
?
-
folate conjugase in the brush-border may accomplish the initial digestion of the dietary pteroylpolyglutamates
-
-
?
pteroylpolyglutamate + H2O
?
-
the enzyme progressively hydrolyzes glutamyl units from pteroylpolyglutamate, leaving pteroylmonoglutamate as the folate form available for intestinal transport
-
-
?
pteroylpolyglutamate + H2O
?
-
possible contribution of biliary enzyme to intestinal absorption of folate polyglutamates
-
-
?
pteroylpolyglutamate + H2O
?
-
pancreatic enzyme may act in vivo in folate digestion and absorption to initiate the deconjugation of dietary pteroylpolyglutamate prior to the action of jejunal brush-border enzyme
-
-
?
pteroyltriglutamate + H2O
?
-
-
-
-
?
pteroyltriglutamate + H2O
?
-
-
-
-
?
pteroyltriglutamate + H2O
?
-
-
-
-
?
pteroyltriglutamate + H2O
?
-
-
-
-
?
pteroyltriglutamate + H2O
?
-
-
-
-
?
pteroyltriglutamate + H2O
pteroylglutamate + glutamate
-
-
-
-
?
pteroyltriglutamate + H2O
pteroylglutamate + glutamate
-
-
-
-
?
pteroyltriglutamate + H2O
pteroylglutamate + glutamate
-
-
-
?
pteroyltriglutamate + H2O
pteroylglutamate + glutamate
-
-
+ pteroyldiglutamate
?
pteroyltriglutamate + H2O
pteroylglutamate + glutamate
-
-
-
-
?
pteroyltriglutamate + H2O
pteroylglutamate + glutamate
-
-
-
-
?
pteroyltriglutamate + H2O
pteroylglutamate + glutamate
-
-
-
?
additional information
?
-
isoform GGH2 alone is able to completely deconjugate folates using 50-100 microg/g of sample for 1 h at 37°C in all matrices tested. It removes the tails of folylpolyglutamates from tomato fruit, black bean and peanut seeds, and alfalfa sprouts extracts
-
-
?
additional information
?
-
-
the enzyme specifically cleaves D- and L-polyglutamic acid, preferred to entirely of poly-D-glutamic acid, a component of the capsule produced by several strains of Bacillus subtilis, the enzyme has minimal activity in degrading Bacillus anthracis and to remove the capsule from the surface of bacilli, the poly-gamma-D-glutamic acid capsule, no effect on RAW264.7 murine macrophage phagocytosis, and only minimal enhancement of human host neutrophil killing
-
-
?
additional information
?
-
-
the enzyme hydrolyzes synthetically hydrolyzed oligo-gamma-L-glutamates, but not oligo-gamma-D-glutamates, and degrades polyglutamic acid to a hydrolyzed product of about 20 kDa with a ratio of D- and L-glutamic acids of 70:30, thus the enzyme cleaves the bond between two L-glutamic acid residues, overview
-
-
?
additional information
?
-
hydrolysis of the gamma-glutamate bond, resulting in folate-mono-Glu
-
-
?
additional information
?
-
-
hydrolysis of the gamma-glutamate bond, resulting in folate-mono-Glu
-
-
?
additional information
?
-
hydrolysis of the gamma-glutamate bond, resulting in folate-mono-Glu
-
-
?
additional information
?
-
-
no hydrolysis of alpha-glutamyl peptides
-
-
?
additional information
?
-
-
enzyme does not show any transpeptidase activity
-
-
?
additional information
?
-
-
enzyme does not show any transpeptidase activity
-
-
?
additional information
?
-
-
the maximal velocity decreases in the order methothrexate hexaglutamate, methotrexate tetraglutamate, methotrexate pentaglutamate, methotrexate triglutamate
-
-
?
additional information
?
-
-
soluble enzyme has a requirement for sulfhydryl groups in the active site
-
-
?
additional information
?
-
-
the intracellular enzyme shows the greatest affinity for the complete folic acid molecule with longer glutamate chains
-
-
?
additional information
?
-
-
the enzyme is a cysteine peptidase
-
-
?
additional information
?
-
-
the intracellular enzyme cleaves both terminal and internal gamma-glutamate linkages, in contrast the brush-border enzyme catalyzes the hydrolysis of only terminal gamma-glutamate linkages
-
-
?
additional information
?
-
-
progressively removes gamma-glutamyl residues at acidic pH from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free gamma-glutamic acid, highly specific for the gamma-glutamyl bond, but not for the C-terminal amino acid (leaving group), action on gamma-glutamyl bonds is independent of an N-terminal pteroyl moiety
-
-
?
additional information
?
-
-
GGH catalyzes degradation of the active polyglutamates of natural folates and the antifolate methotrexate
-
-
?
additional information
?
-
-
key enzyme in the metabolism of folic acid and the pharmacology of many antifolate drugs
-
-
?
additional information
?
-
the CpG island methylator phenotype in colorectal cancer is defined as concomitant and frequent hypermethylation of CpG islands within gene promoter regions, and is correlated with low expression levels of the enzyme in primary cancer cells, GGH is involved in the folate pathway and in the development and/or progression of this phenotype, CIMP+-related clinicopathological and molecular features, overview
-
-
?
additional information
?
-
-
the enzyme cleaves gamma-polyglutamate chains attached to folates and anti-folates after they enter mammalian cells, the enzyme plays an important role in folate homeostasis and confers resistance to anti-folates, especially methotrexate, the drugs are dependent on polyglutamylation for activity, overview
-
-
?
additional information
?
-
-
the enzyme cleaves gamma-polyglutamate chains attached to folates and anti-folates after they enter mammalian cells, the enzyme plays an important role in folate homeostasis and confers resistance to anti-folates, especially methotrexate
-
-
?
additional information
?
-
-
no hydrolysis of gamma-glutamyl tripeptide
-
-
?
additional information
?
-
-
no hydrolysis of N-carbobenzoxyphenylalanyl-alanine
-
-
?
additional information
?
-
-
endopeptidase activity
-
-
?
additional information
?
-
-
no hydrolysis of poly-alpha-glutamate
-
-
?
additional information
?
-
-
protein-associated poly-gamma-glutamates are poor substrates
-
-
?
additional information
?
-
-
no hydrolysis of 4-amino-benzoyl-gamma-glutamate
-
-
?
additional information
?
-
key enzyme in the metabolism of folic acid and the pharmacology of many antifolate drugs
-
-
?
additional information
?
-
-
the enzyme cleaves gamma-polyglutamate chains attached to folates and anti-folates after they enter mammalian cells, the enzyme plays an important role in folate homeostasis and confers resistance to anti-folates, especially methotrexate
-
-
?
additional information
?
-
-
either deacylation or rearrangement of the enzyme-product complex is rate-limiting in the isopeptide hydrolysis reaction
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase
-
-
?
additional information
?
-
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than p-aminobenzoylpentaglutamate
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than p-aminobenzoylpentaglutamate
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than p-aminobenzoylpentaglutamate
-
-
?
additional information
?
-
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than p-aminobenzoylpentaglutamate
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than pABAGlu5
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than pABAGlu5
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than pABAGlu5
-
-
?
additional information
?
-
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than pABAGlu5
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
folate + H2O
pteroate + glutamate
-
-
-
-
?
folic acid pentaglutamate + H2O
?
PteGlu5
-
-
?
p-aminobenzoylpentaglutamate + H2O
?
pABAGlu5
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
pteroylpolyglutamate + H2O
?
additional information
?
-
glutathione + H2O
?
-
enzyme hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress
-
-
?
glutathione + H2O
?
-
enzyme hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
-
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
-
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
-
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
-
-
?
polyglutamyl-folate + H2O
monoglutamyl folate + glutamate
-
gamma-glutamyl hydrolase, not glutamate carboxypeptidase II, hydrolyzes dietary folate in rat small intestine
-
-
?
pteroylpolyglutamate + H2O
?
-
the enzyme is responsible for the intracellular cleavage of poly-gamma-glutamates
-
-
?
pteroylpolyglutamate + H2O
?
-
the enzyme is suggested to be involved in the destruction of microorganisms in granulocytes during phagocytosis
-
-
?
pteroylpolyglutamate + H2O
?
-
central enzyme in folyl and antifolylpoly-gamma-glutamate metabolism
-
-
?
pteroylpolyglutamate + H2O
?
-
key enzyme in the maintenance of cellular folylpolyglutamate concentration
-
-
?
pteroylpolyglutamate + H2O
?
-
central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism
-
-
?
pteroylpolyglutamate + H2O
?
-
folate conjugase in the brush-border may accomplish the initial digestion of the dietary pteroylpolyglutamates
-
-
?
pteroylpolyglutamate + H2O
?
-
the enzyme progressively hydrolyzes glutamyl units from pteroylpolyglutamate, leaving pteroylmonoglutamate as the folate form available for intestinal transport
-
-
?
pteroylpolyglutamate + H2O
?
-
possible contribution of biliary enzyme to intestinal absorption of folate polyglutamates
-
-
?
pteroylpolyglutamate + H2O
?
-
pancreatic enzyme may act in vivo in folate digestion and absorption to initiate the deconjugation of dietary pteroylpolyglutamate prior to the action of jejunal brush-border enzyme
-
-
?
additional information
?
-
-
the enzyme specifically cleaves D- and L-polyglutamic acid, preferred to entirely of poly-D-glutamic acid, a component of the capsule produced by several strains of Bacillus subtilis, the enzyme has minimal activity in degrading Bacillus anthracis and to remove the capsule from the surface of bacilli, the poly-gamma-D-glutamic acid capsule, no effect on RAW264.7 murine macrophage phagocytosis, and only minimal enhancement of human host neutrophil killing
-
-
?
additional information
?
-
hydrolysis of the gamma-glutamate bond, resulting in folate-mono-Glu
-
-
?
additional information
?
-
-
hydrolysis of the gamma-glutamate bond, resulting in folate-mono-Glu
-
-
?
additional information
?
-
hydrolysis of the gamma-glutamate bond, resulting in folate-mono-Glu
-
-
?
additional information
?
-
-
GGH catalyzes degradation of the active polyglutamates of natural folates and the antifolate methotrexate
-
-
?
additional information
?
-
-
key enzyme in the metabolism of folic acid and the pharmacology of many antifolate drugs
-
-
?
additional information
?
-
the CpG island methylator phenotype in colorectal cancer is defined as concomitant and frequent hypermethylation of CpG islands within gene promoter regions, and is correlated with low expression levels of the enzyme in primary cancer cells, GGH is involved in the folate pathway and in the development and/or progression of this phenotype, CIMP+-related clinicopathological and molecular features, overview
-
-
?
additional information
?
-
-
the enzyme cleaves gamma-polyglutamate chains attached to folates and anti-folates after they enter mammalian cells, the enzyme plays an important role in folate homeostasis and confers resistance to anti-folates, especially methotrexate, the drugs are dependent on polyglutamylation for activity, overview
-
-
?
additional information
?
-
-
the enzyme cleaves gamma-polyglutamate chains attached to folates and anti-folates after they enter mammalian cells, the enzyme plays an important role in folate homeostasis and confers resistance to anti-folates, especially methotrexate
-
-
?
additional information
?
-
key enzyme in the metabolism of folic acid and the pharmacology of many antifolate drugs
-
-
?
additional information
?
-
-
the enzyme cleaves gamma-polyglutamate chains attached to folates and anti-folates after they enter mammalian cells, the enzyme plays an important role in folate homeostasis and confers resistance to anti-folates, especially methotrexate
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase
-
-
?
additional information
?
-
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than p-aminobenzoylpentaglutamate
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than p-aminobenzoylpentaglutamate
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than p-aminobenzoylpentaglutamate
-
-
?
additional information
?
-
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than p-aminobenzoylpentaglutamate
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than pABAGlu5
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than pABAGlu5
-
-
?
additional information
?
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than pABAGlu5
-
-
?
additional information
?
-
-
folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than pABAGlu5
-
-
?
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Arthritis, Rheumatoid
Erythrocyte methotrexate-polyglutamate assay using fluorescence polarization immunoassay technique: application to the monitoring of patients with rheumatoid arthritis.
Breast Neoplasms
Folate conjugase activity in the plasma and tumors of breast-cancer patients.
Breast Neoplasms
Identification of single nucleotide polymorphisms in the human gamma-glutamyl hydrolase gene and characterization of promoter polymorphisms.
Breast Neoplasms
Membrane Glycoproteins Associated with Breast Tumor Cell Progression Identified by a Lectin Affinity Approach.
Breast Neoplasms
Secretion of gamma-glutamyl hydrolase in vitro.
Carcinoma
Overexpression, genomic amplification and therapeutic potential of inhibiting the UbcH10 ubiquitin conjugase in human carcinomas of diverse anatomic origin.
Carcinoma, Ductal
Folate conjugase activity in the plasma and tumors of breast-cancer patients.
Carcinoma, Hepatocellular
Effects of gamma-glutamyl hydrolase on folyl and antifolylpolyglutamates in cultured H35 hepatoma cells.
Carcinoma, Hepatocellular
Identification, cloning, and sequencing of a cDNA coding for rat gamma-glutamyl hydrolase.
Carcinoma, Hepatocellular
Secretion of gamma-glutamyl hydrolase in vitro.
Carcinoma, Hepatocellular
The properties and function of gamma-glutamyl hydrolase and poly-gamma-glutamate.
Carcinoma, Hepatocellular
The properties of the secreted gamma-glutamyl hydrolases from H35 hepatoma cells.
Carcinoma, Hepatocellular
The role of folylpolyglutamate synthetase and gamma-glutamyl hydrolase in altering cellular folyl- and antifolylpolyglutamates.
Celiac Disease
Jejunal perfusion of simple and conjugated folates in celiac sprue.
Celiac Disease
The folate conjugase activity of the intestinal mucosa in celiac disease.
Choriocarcinoma
Secretion of gamma-glutamyl hydrolase in vitro.
Colorectal Neoplasms
Altered gene expression of folate enzymes in adjacent mucosa is associated with outcome of colorectal cancer patients.
Colorectal Neoplasms
Low expression of gamma-glutamyl hydrolase mRNA in primary colorectal cancer with the CpG island methylator phenotype.
Fanconi Anemia
Deficiency of the Fanconi anemia E2 ubiqitin conjugase UBE2T only partially abrogates Alu-mediated recombination in a new model of homology dependent recombination.
Fibroadenoma
Folate conjugase activity in the plasma and tumors of breast-cancer patients.
folate gamma-glutamyl hydrolase deficiency
Significance of subnormal red-cell folate in thalassaemia.
Glioblastoma
Overexpression, genomic amplification and therapeutic potential of inhibiting the UbcH10 ubiquitin conjugase in human carcinomas of diverse anatomic origin.
Immune System Diseases
UBE2N Promotes Melanoma Growth via MEK/FRA1/SOX10 Signaling.
Iron Deficiencies
A lysine-63-linked ubiquitin chain-forming conjugase, UBC13, promotes the developmental responses to iron deficiency in Arabidopsis roots.
Leukemia
gamma-Glutamyl hydrolase and folylpolyglutamate synthetase activities predict polyglutamylation of methotrexate in acute leukemias.
Leukemia
Honokiol induces proteasomal degradation of AML1-ETO oncoprotein via increasing ubiquitin conjugase UbcH8 expression in leukemia.
Leukemia
Identification of single nucleotide polymorphisms in the human gamma-glutamyl hydrolase gene and characterization of promoter polymorphisms.
Leukemia
Role of folylpolyglutamate synthetase and folylpolyglutamate hydrolase in methotrexate accumulation and polyglutamylation in childhood leukemia.
Leukemia
Secretion of gamma-glutamyl hydrolase in vitro.
Leukemia
[Separation of methotrexate-polyglutamates by capillary electrophoresis and its application to the measurement of gamma-glutamyl hydrolase activity in human leukemia cells in culture]
Lung Neoplasms
Gamma-glutamyl hydrolase and drug resistance.
Melanoma
UBE2N Promotes Melanoma Growth via MEK/FRA1/SOX10 Signaling.
Multiple Myeloma
Amplification and overexpression of E2 ubiquitin conjugase UBE2T promotes homologous recombination in multiple myeloma.
Neoplasms
A novel class of monoglutamated antifolates exhibits tight-binding inhibition of human glycinamide ribonucleotide formyltransferase and potent activity against solid tumors.
Neoplasms
A randomized, double-blind, phase II study of two doses of pemetrexed as first-line chemotherapy for advanced breast cancer.
Neoplasms
Altered gene expression of folate enzymes in adjacent mucosa is associated with outcome of colorectal cancer patients.
Neoplasms
Characterization of human cellular gamma-glutamyl hydrolase.
Neoplasms
Characterization of the human gamma-glutamyl hydrolase promoter and its gene expression in human tissues and cancer cell lines.
Neoplasms
Folate conjugase activity in the plasma and tumors of breast-cancer patients.
Neoplasms
Gamma-glutamyl hydrolase and drug resistance.
Neoplasms
Gene expression levels of gamma-glutamyl hydrolase in tumor tissues may be a useful biomarker for the proper use of S-1 and tegafur-uracil/leucovorin in preoperative chemoradiotherapy for patients with rectal cancer.
Neoplasms
Hydrolytic cleavage of methotrexate gamma-polyglutamates by folylpolyglutamyl hydrolase derived from various tumors and normal tissues of the mouse.
Neoplasms
Karyotypic abnormalities create discordance of germline genotype and cancer cell phenotypes.
Neoplasms
Overexpression, genomic amplification and therapeutic potential of inhibiting the UbcH10 ubiquitin conjugase in human carcinomas of diverse anatomic origin.
Neoplasms
Predicting clinical outcome of 5-fluorouracil-based chemotherapy for colon cancer patients: is the CpG island methylator phenotype the 5-fluorouracil-responsive subgroup?
Neoplasms
Tumor-related gene expression levels in thymic carcinoma and Type B3 thymoma.
Neoplasms
UBE2N Promotes Melanoma Growth via MEK/FRA1/SOX10 Signaling.
Neoplasms
[Separation of methotrexate-polyglutamates by capillary electrophoresis and its application to the measurement of gamma-glutamyl hydrolase activity in human leukemia cells in culture]
Neuroendocrine Tumors
Identification of carboxypeptidase E and gamma-glutamyl hydrolase as biomarkers for pulmonary neuroendocrine tumors by cDNA microarray.
Parkinson Disease
The SUMO Conjugase Ubc9 Protects Dopaminergic Cells from Cytotoxicity and Enhances the Stability of ?-Synuclein in Parkinson's Disease Models.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Epigenetic regulation of human gamma-glutamyl hydrolase activity in acute lymphoblastic leukemia cells.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Influence of genetic polymorphisms of FPGS, GGH, and MTHFR on serum methotrexate levels in Chinese children with acute lymphoblastic leukemia.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Methotrexate intracellular disposition in acute lymphoblastic leukemia: a mathematical model of gamma-glutamyl hydrolase activity.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Polymorphisms of the gamma-glutamyl hydrolase gene and risk of relapse to acute lymphoblastic leukemia in Mexico.
Precursor T-Cell Lymphoblastic Leukemia-Lymphoma
Role of folylpolyglutamate synthetase and folylpolyglutamate hydrolase in methotrexate accumulation and polyglutamylation in childhood leukemia.
Psoriasis
Outcomes of methotrexate therapy for psoriasis and relationship to genetic polymorphisms.
Rectal Neoplasms
Gene expression levels of gamma-glutamyl hydrolase in tumor tissues may be a useful biomarker for the proper use of S-1 and tegafur-uracil/leucovorin in preoperative chemoradiotherapy for patients with rectal cancer.
Sarcoma
gamma-Glutamyl hydrolase from human sarcoma HT-1080 cells: characterization and inhibition by glutamine antagonists.
Sarcoma
Increased activity of gamma-glutamyl hydrolase in human sarcoma cell lines: a novel mechanism of intrinsic resistance to methotrexate (MTX).
Sprue, Tropical
Folic acid conjugase in normal human plasma and in the plasma of patients with tropical sprue.
Sprue, Tropical
Intestinal folate conjugase activity in tropical sprue.
Stomach Neoplasms
High gamma-glutamyl hydrolase and low folylpolyglutamate synthetase expression as prognostic biomarkers in patients with locally advanced gastric cancer who were administrated postoperative adjuvant chemotherapy with S-1.
Tuberculosis, Pulmonary
Serum protein gamma-glutamyl hydrolase, Ig gamma-3 chain C region, and haptoglobin are associated with the syndromes of pulmonary tuberculosis in traditional Chinese medicine.
Vitamin B 12 Deficiency
Significance of subnormal red-cell folate in thalassaemia.
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Rao, K.N.; Noronha, J.M.
Studies on the enzymatic hydrolysis of polyglutamyl folates by chicken liver folyl poly-gamma-glutamyl carboxypeptidase. I. Intracellular localization, purification and partial characterization of the enzyme
Biochim. Biophys. Acta
481
594-607
1977
Gallus gallus
brenda
Rao, K.N.; Noronha, J.M.
Studies on the enzymatic hydrolysis of polyglutamyl folates by chicken liver folyl poly-gamma-glutamyl carboxypeptidase. II. Structural studies
Biochim. Biophys. Acta
481
608-616
1977
Gallus gallus
brenda
Elsenhans, B.; Ahmad, O.; Rosenberg, I.H.
Isolation and characterization of pteroylpolyglutamate hydrolase from rat intestinal mucosa
J. Biol. Chem.
259
6364-6368
1984
Rattus norvegicus
brenda
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
brenda
Silink, M.; Reddel, R.; Bethel, M.; Rowe, P.B.
Gamma-glutamyl hydrolase conjugase. Purification and properties of the bovine hepatic enzyme
J. Biol. Chem.
250
5982-5994
1975
Bos taurus
brenda
Lakshmaiah, N.; Ramasastri, B.V.
Plasma folic acid conjugase
Methods Enzymol.
66
670-678
1980
Homo sapiens
brenda
Reisenauer, A.M.
Folate conjugase: two separate activities in human jejunum
Science
198
196-197
1977
Homo sapiens
brenda
Muro, T.; Nagamori, Y.; Okada, S.; Tominaga, Y.
Some properties and action of poly(glutamic acid) hydrolase II from Micromonospora melanosporea IFO 12515
Agric. Biol. Chem.
54
1065-1067
1990
Micromonospora melanosporea
brenda
Lin, S.; Rogiers, S.; Cossins, E.A.
gamma-Glutamyl hydrolase from pea cotyledons
Phytochemistry
32
1109-1117
1993
Pisum sativum
-
brenda
Wang, Y.; Nimec, Z.; Ryan, T.J.; Dias, J.A.; Galivan, J.
The properties of the secreted gamma-glutamyl hydrolases from H35 hepatoma cells
Biochim. Biophys. Acta
1164
227-235
1993
Rattus norvegicus
brenda
Tanaka, T.; Hiruta, O.; Futamura, T.; Uotani, K.; Satoh, A.; Taniguchi, M.; Or, S.
Purification and characterization of poly(g-glutamic acid) hydrolase from a filamentous fungus, Myrothecium sp. TM-4222
Biosci. Biotechnol. Biochem.
57
2148-2153
1993
Myrothecium sp., Myrothecium sp. TM-4222
-
brenda
Kferstein, H.; Jaenicke, L.
Gamma glutamyl carboxypeptidase from chicken pancreas
Hoppe-Seyler's Z. Physiol. Chem.
353
1153-1158
1972
Gallus gallus
brenda
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
brenda
Horne, D.W.; Krumdieck, C.L.; Wagner, C.
Properties of folic acid gamma-glutamyl hydrolase (conjugase) in rat bile and plasma
J. Nutr.
111
442-449
1981
Rattus norvegicus
brenda
Hartley, D.M.; Snodgrass, S.R.; Bradshaw, P.A.
The measurement of gamma-glutamyl hydrolase (conjugase) activity in rat brain
Neurochem. Res.
13
147-151
1988
Rattus norvegicus
brenda
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
brenda
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
brenda
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
brenda
Krungkrai, J.; Yuthavong, Y.; Webster, H.K.
High-performance liquid chromatographic assay for pteroylpolyglutamate hydrolase
J. Chromatogr.
417
47-56
1987
Homo sapiens
brenda
Elsenhans, B.; Selhub, J.; Rosenberg, I.H.
Assay of folylpolyglutamate hydrolase using pteroyl-labeled substrates and selective short-term bacterial uptake for product determination
Methods Enzymol.
66
663-666
1980
Rattus norvegicus
brenda
Rosenberg, I.H.; Saini, P.K.
Folylpolyglutamate endopeptidase from chicken intestine: isolation with the aid of affinity chromatography
Methods Enzymol.
66
667-670
1980
Gallus gallus
brenda
Leichter, J.; Butterworth, C.E.Jr.; Krumdieck, C.L.
Partial purification and some properties of pteroylpolyglutamate hydrolase (conjugase) from chicken pancreas
Proc. Soc. Exp. Biol. Med.
154
98-101
1977
Gallus gallus
brenda
Bhandari, S.D.; Gregory, J.F.3rd.; Renuart, D.R.; Merritt, A.M.
Properties of pteroylpolyglutamate hydrolase in pancreatic juice of the pig
J. Nutr.
120
467-475
1990
Sus scrofa
brenda
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
brenda
Samuels, L.L.; Goutas, L.J.; Priest, D.G.; Piper, J.R.; Sirotnak, F.M.
Hydrolytic cleavage of methotrexate gamma-polyglutamates by folylpolyglutamyl hydrolase derived from various tumors and normal tissues of the mouse
Cancer Res.
46
2230-2235
1986
Mus musculus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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 substrate
J. Biol. Chem.
277
24522-24529
2002
Homo sapiens
brenda
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
brenda
Orsomando, G.; de la Garza, R.D.; Green, B.J.; Peng, M.; Rea, P.A.; Ryan, T.J.; Gregory, J.F.; Hanson, A.D.
Plant gamma-glutamyl hydrolases and folate polyglutamates: characterization, compartmentation, and co-occurrence in vacuoles
J. Biol. Chem.
280
28877-28884
2005
Beta vulgaris, Pisum sativum, Arabidopsis thaliana (O65355)
brenda
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
brenda
Scorpio, A.; Chabot, D.J.; Day, W.A.; Obrien, D.K.; Vietri, N.J.; Itoh, Y.; Mohamadzadeh, M.; Friedlander, A.M.
Poly-gamma-glutamate capsule-degrading enzyme treatment enhances phagocytosis and killing of encapsulated Bacillus anthracis
Antimicrob. Agents Chemother.
51
215-222
2007
Bacillus phage phiNIT1
brenda
Alexander, J.P.; Ryan, T.J.; Ballou, D.P.; Coward, J.K.
Gamma-glutamyl hydrolase: kinetic characterization of isopeptide hydrolysis using fluorogenic substrates
Biochemistry
47
1228-1239
2008
Rattus norvegicus
brenda
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)
brenda
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
brenda
Chunhachart, O.; Itoh, T.; Sukchotiratana, M.; Tanimoto, H.; Tahara, Y.
Characterization of gamma-glutamyl hydrolase produced by Bacillus sp. isolated from Thai Thua-nao
Biosci. Biotechnol. Biochem.
70
2779-2782
2006
Bacillus sp. (in: Bacteria)
brenda
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)
brenda
Schneider, E.; Ryan, T.J.
Gamma-glutamyl hydrolase and drug resistance
Clin. Chim. Acta
374
25-32
2006
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Chen, L.; Eitenmiller, R.R.
Optimization of the trienzyme extraction for the microbiological assay of folate in vegetables
J. Agric. Food Chem.
55
3884-3888
2007
Gallus gallus
brenda
Shafizadeh, T.B.; Halsted, C.H.
gamma-Glutamyl hydrolase, not glutamate carboxypeptidase II, hydrolyzes dietary folate in rat small intestine
J. Nutr.
137
1149-1153
2007
Rattus norvegicus
brenda
Kao, T.T.; Chang, W.N.; Wu, H.L.; Shi, G.Y.; Fu, T.F.
Recombinant zebrafish gamma-glutamyl hydrolase exhibits properties and catalytic activities comparable with those of mammalian enzyme
Drug Metab. Dispos.
37
302-309
2009
Danio rerio (Q6NY42), Danio rerio, Danio rerio AB (Q6NY42)
brenda
Akhtar, T.A.; McQuinn, R.P.; Naponelli, V.; Gregory, J.F.; Giovannoni, J.J.; Hanson, A.D.
Tomato gamma-glutamylhydrolases: expression, characterization, and evidence for heterodimer formation
Plant Physiol.
148
775-785
2008
Solanum lycopersicum (B2Z9Y3), Solanum lycopersicum (B2Z9Y4), Solanum lycopersicum (B2Z9Y5), Solanum lycopersicum
brenda
Castellano, I.; Merlino, A.; Rossi, M.; La Cara, F.
Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity
Biochimie
92
464-474
2010
Geobacillus thermodenitrificans
brenda
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
brenda
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 (Q92820), Homo sapiens
brenda
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
brenda
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
brenda
Tsirulnikov, K.; Abuladze, N.; Bragin, A.; Faull, K.; Cascio, D.; Damoiseaux, R.; Schibler, M.J.; Pushkin, A.
Inhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal
Toxicol. Appl. Pharmacol.
263
303-314
2012
Mus musculus
brenda
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
brenda
Ramos-Parra, P.; Urrea-Lopez, R.; Diaz de la Garza, R.
Folate analysis in complex food matrices: Use of a recombinant Arabidopsis ?-glutamyl hydrolase for folate deglutamylation
Food Res. Int.
54
177-185
2013
Arabidopsis thaliana (O65355)
brenda
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
brenda
Chuankhayan, P.; Kao, T.T.; Lin, C.C.; Guan, H.H.; Nakagawa, A.; Fu, T.F.; Chen, C.J.
Structural insights into the hydrolysis and polymorphism of methotrexate polyglutamate by zebrafish gamma-glutamyl hydrolase
J. Med. Chem.
56
7625-7635
2013
Danio rerio (Q6NY42)
brenda
Fujimoto, Z.; Kimura, K.
Crystal structure of bacteriophage phiNIT1 zinc peptidase PghP that hydrolyzes gamma-glutamyl linkage of bacterial poly-gamma-glutamate
Proteins Struct. Funct. Bioinform.
80
722-732
2012
Bacillus phage phiNIT1 (Q852V1)
brenda