3.4.19.9: folate gamma-glutamyl hydrolase
This is an abbreviated version!
For detailed information about folate gamma-glutamyl hydrolase, go to the full flat file.
Word Map on EC 3.4.19.9
-
3.4.19.9
-
polyglutamates
-
methotrexate
-
polyglutamylation
-
antifolate
-
casei
-
monoglutamates
-
pteroylpolyglutamate
-
sumo
-
monoglutamylated
-
5-methyltetrahydrofolate
-
deconjugation
-
trienzyme
-
pentaglutamate
-
rad6
-
diglutamate
-
punicic
-
medicine
-
analysis
- 3.4.19.9
- polyglutamates
- methotrexate
-
polyglutamylation
- antifolate
- casei
- monoglutamates
- pteroylpolyglutamate
- sumo
-
monoglutamylated
- 5-methyltetrahydrofolate
-
deconjugation
-
trienzyme
- pentaglutamate
- rad6
- diglutamate
-
punicic
- medicine
- analysis
Reaction
Synonyms
At1g78680, AtGGH1, AtGGH2, carboxypeptidase G, conjugase, EC 3.4.12.10, EC 3.4.22.12, FGPH, folate conjugase, folate hydrolase, folic acid conjugase, folylpolyglutamate hydrolase, gamma-GH, gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, gamma-polyglutamic acid hydrolase, gammaGH, GGH, GGH2, hydrolase, gamma-glutamyl, LeGGH1, LeGGH2, LeGGH3, low gamma-glutamyl hydrolase, lysosomal gamma-glutamyl carboxypeptidase, PghP, poly(gamma-glutamic acid) endohydrolase, poly(glutamic acid) hydrolase II, polyglutamate hydrolase, pteroyl-poly-gamma-glutamate hydrolase, pteroylpoly-gamma-glutamyl hydrolase, zgammaGH
ECTree
3.4.19.9 folate gamma-glutamyl hydrolaseAdvanced search results
results (
results (Natural Substrates Products
Natural Substrates Products on EC 3.4.19.9 - folate gamma-glutamyl hydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
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
p-aminobenzoylpentaglutamate + H2O
?
pABAGlu5
-
-
?
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
-
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
-
-
?
