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3.4.17.21: Glutamate carboxypeptidase II

This is an abbreviated version!
For detailed information about Glutamate carboxypeptidase II, go to the full flat file.

Word Map on EC 3.4.17.21

Reaction

release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates =

Synonyms

100 kDa ileum brush border membrane protein, Acetylaspartylglutamate dipeptidase, altered meristem program1, AMP1, Dipeptidase, acetylaspartylglutamate, EC 3.4.19.8, FGCP, folate hydrolase, folate hydrolase 1, FOLH1, Folylpoly-gamma-glutamate carboxypeptidase, folylpoly-gamma-glutamate carboxypeptidase II, GCP II, GCPII, GCPIII, glutamate carboxypeptidase, glutamate carboxypeptidase II, glutamate carboxypeptidase III, GPCPII, I100, Ileal dipeptidylpeptidase, Membrane glutamate carboxypeptidase, mGCP, More, N-acetyl-alpha-linked acidic dipeptidase, N-acetyl-alpha-linked acidic dipeptidase I, N-acetylaspartylglutamate peptidase, N-acetylated alpha-linked acid dipeptidase, N-Acetylated alpha-linked acidic dipeptidase, N-Acetylated-alpha-linked acidic dipeptidase, N-acetylated-alpha-linked acidic dipeptidase 2, N-acetylated-alpha-linked acidic dipeptidase II, N-Acetylated-alpha-linked-acidic dipeptidase, N-acetylated-alpha-linked-acidic-dipeptidase, N-Acetylated-alpha-linked-amino dipeptidase, NAADLADase, NAADLADse, NAAG degradation enzyme, NAAG peptidase, NAAG peptidase II, NAAG-hydrolyzing activity, NAALA dipeptidase, NAALADase, Naaladase I, NAALADase II, NLD I, PMSA, prostate specific membrane antigen, Prostate-specific membrane antigen, Prostate-specific membrane antigen homolog, prostate-specificmembrane antigen, Prostrate-specific membrane antigen, PSM, PSM antigen, PSMA, Pteroylpoly-gamma-glutamate carboxypeptidase, Rat NAAG peptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.21 Glutamate carboxypeptidase II

Engineering

Engineering on EC 3.4.17.21 - Glutamate carboxypeptidase II

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA1-42
-
the recombinantly expressed extracellular domain has a cytosolic localization compared to sell surface membrane localization of the full-length enzyme. Less than 5% of the activity of the wild-type enzyme
DELTA20-42
-
mutant enzyme omitting the transmembrane domain is associated with the cell surface membrane as is the full-length enzyme. Less than 5% of the activity of the wild-type enzyme
E424A
H380G
-
site-directed mutagenesis, active site mutant, inactive mutant
H475Y
K479R
in the presence of cycloheximide the mutant is less ubiquitinylated and degraded. Decrease in the level of glutamate carboxypeptidase II protein by histone deacetylase is significantly blocked by K479R mutants
K491R
in the presence of cycloheximide the mutant is less ubiquitinylated and degraded
L4A/L5A
-
site-directed mutagenesis, internalization motif mutant, active mutant, no endocytic internalization
N121A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
N140A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
N153A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
N195A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
N336A
N459A
-
site-directed mutagenesis, glycosylation site E mutant, inactive mutant, no endocytic internalization
N476A
N51A
-
site-directed mutagenesis of an N-glycosylation site leads to 75% reduced activity compared to the wild-type enzyme
N638A
N76A
-
site-directed mutagenesis of an N-glycosylation site leads to 25% reduced activity compared to the wild-type enzyme
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
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
T640A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
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
additional information