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Literature summary for 3.4.17.21 extracted from

  • Navratil, M.; Ptacek, J.; Sacha, P.; Starkova, J.; Lubkowski, J.; Bakinka, C.; Konvalinka, J.
    Structural and biochemical characterization of the folyl-poly-gamma-L-glutamate hydrolyzing activity of human glutamate carboxypeptidase II (2014), FEBS J., 281, 3228-3242.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Drosophila S2 cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray structures of seven complexes of the hydrolytically inactive recombinant E424A mutant and polyglutamylated folates substrates, refined at resolutions of between 1.65 and 2.00 A, and mutant H475Y, in complex with substrate N-acetyl-L-aspartyl-L-glutamate to 1.83 A resolution Homo sapiens

Protein Variants

Protein Variants Comment Organism
E424A catalytically inactive, series of X-ray structures of complexes a panel of naturally occurring polyglutamylated folates Homo sapiens
H475Y X-ray structure in complex with substrate N-acetyl-L-aspartyl-L-glutamate,wild-type and the H475 variant are functionally identical. both proteins share an almost identical arrangement of amino acids in the vicinity of residue 475, and the imidazole ring of wild-type His475 and the benzene ring of Tyr475 overlap spatiallyl Homo sapiens
R463L no major differences between the mutant and the wild-type enzyme for the kinetic parameters of folyl-gamma-L-glutamic acid hydrolysis, a slight decrease in KM values for both N-acetyl-L-aspartyl-L-glutamate and folyl-(gamma-L-glutamic acid)2, folyl-(gamma-L-glutamic acid)3, folyl-(gamma-L-glutamic acid)4 Homo sapiens
R511L no major differences between the mutant and the wild-type enzyme for the kinetic parameters of folyl-gamma-L-glutamic acid hydrolysis, a slight decrease in KM values for both N-acetyl-L-aspartyl-L-glutamate and folyl-(gamma-L-glutamic acid)2, folyl-(gamma-L-glutamic acid)3, folyl-(gamma-L-glutamic acid)4 Homo sapiens
W541A no major differences between the mutant and the wild-type enzyme for the kinetic parameters of folyl-gamma-L-glutamic acid hydrolysis, a slight decrease in KM values for both N-acetyl-L-aspartyl-L-glutamate and folyl-(gamma-L-glutamic acid)2, folyl-(gamma-L-glutamic acid)3, folyl-(gamma-L-glutamic acid)4 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q04609
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
folyl-(gamma-L-glutamic acid)2 + H2O
-
Homo sapiens folyl-gamma-L-glutamic acid + L-glutamate
-
?
folyl-(gamma-L-glutamic acid)3 + H2O
-
Homo sapiens folyl-(gamma-L-glutamic acid)2 + L-glutamate
-
?
folyl-(gamma-L-glutamic acid)4 + H2O
-
Homo sapiens folyl-(gamma-L-glutamic acid)3 + L-glutamate
-
?
folyl-gamma-L-glutamic acid + H2O
-
Homo sapiens folate + L-glutamate
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
-
Homo sapiens N-acetyl-L-aspartate + L-glutamate
-
?