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
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3.4.19.9
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polyglutamates
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methotrexate
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polyglutamylation
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antifolate
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casei
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monoglutamates
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pteroylpolyglutamate
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sumo
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monoglutamylated
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5-methyltetrahydrofolate
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deconjugation
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trienzyme
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pentaglutamate
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rad6
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diglutamate
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punicic
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medicine
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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
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Engineering on EC 3.4.19.9 - folate gamma-glutamyl hydrolase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H218N
complete loss of hydrolytic activity. Residue His218 alone suffices to catalyze the hydrolysis of the gamma-glutamate bond in gamma-glutamyl hydrolase
T353A
C124A
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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
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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
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Km-value for methotrexate diglutamate is not significantly different from the Km-value of the wild-type enzyme
E222A
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maximal velocity with methotrexate diglutamate is reduced 6fold relative to the wild-type enzyme
H171N
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maximal velocity with methotrexate diglutamate is reduced 250fold relative to the wild-type enzyme
T127I
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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
T353A
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mutation of the N-terminal residue of the 21 kDa subunit, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action
T353A
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mutation abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action
T353A
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mutation of the N-terminal residue of the 21 kDa subunit, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action
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T353A
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mutation abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action
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additional information
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the recombinant glycosylated enzyme forms very stable dimeric complexes with the recombinant His-tagged rat enzyme, overview
additional information
the enzyme forms very stable dimeric complexes with the glycosylated human enzyme, overview
