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Literature summary for 3.4.19.9 extracted from

  • 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 (2000), J. Biol. Chem., 275, 40365-40370.
    View publication on PubMed
Search for more literature for 3.4.19.9

Protein Variants

Protein Variants Comment Organism
C110A inactive mutant enzyme Homo sapiens
E222A maximal velocity with methotrexate diglutamate is reduced 6fold relative to the wild-type enzyme Homo sapiens
H171N maximal velocity with methotrexate diglutamate is reduced 250fold relative to the wild-type enzyme Homo sapiens
H220A inactive mutant enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0214
-
 methotrexate diglutamate mutant enzyme E222A Homo sapiens
0.02945
-
 methotrexate diglutamate wild-type enzyme Homo sapiens
0.0299
-
 methotrexate diglutamate mutant enzyme H171N Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pteroylpolyglutamate + H2O Homo sapiens central enzyme in folyl and antifolylpoly-gamma-glutamate metabolism ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme expressed in Escherichia coli Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methotrexate diglutamate + H2O
-
 Homo sapiens ?
-
 ?
pteroylpolyglutamate + H2O central enzyme in folyl and antifolylpoly-gamma-glutamate metabolism Homo sapiens ?
-
 ?