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.

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

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Results	in table
1	Activating Compound
189	AA Sequence
40	Application
1	CAS Registry Number
25	Cloned(Commentary)
12	Crystallization (Commentary)
7461	Disease/ Diagnostics
5	Expression
9	General Information
3	General Stability
121	IC50 Value
374	Inhibitors
4	kcat/KM [mM/s]
108	Ki Value [mM]
15	KM Value [mM]
83	Localization
41	Metals/Ions
8	Molecular Weight [Da]
62	Natural Substrates/ Products (Substrates)
128	Organism
2	Pathway
90	PDB ID
15	pH Optimum
2	pH Range
17	Posttranslational Modification
37	Protein Variants
14	Purification (Commentary)
4	Reaction
7	Reaction Type
126	Reference
230	Source Tissue
10	Specific Activity [micromol/min/mg]
144	Substrates and Products (Substrate)
10	Subunits
261	Synonyms
14	Temperature Optimum [°C]
1	Temperature Range [°C]
6	Turnover Number [1/s]

General Information

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General Information on EC 3.4.17.21 - Glutamate carboxypeptidase II

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

3 entries

metabolism

Homo sapiens

Q04609

acute exposure to valproic acid, a drug used for bipolar disorder and epilepsy and a known histone deacetylase inhibitor, for 4-6 h increases the glutamate carboxypeptidase II protein level in human astrocyte U-87MG cells but does not have a similar effect after 12-24 h exposure. Valproic acid does not affect the glutamate carboxypeptidase II mRNA expression, but decrease in glutamate carboxypeptidase II protein level by cycloheximide treatment is blocked by valproic acid. The valproic acid-induced increase of glutamate carboxypeptidase II protein level may be dependent on the ubiquitin/proteasome pathway. Valproic acid increases the acetylation of glutamate carboxypeptidase II protein at the lysine residues and facilitates a decrease of the poly-ubiquitinated glutamate carboxypeptidase II level. Similarly, M344, a specific histone deacetylase 1/6 inhibitor, also increases the glutamate carboxypeptidase II protein level

731257

physiological function

5 entries

malfunction

Homo sapiens

-

inhibition of the GCP II-catalyzed reaction is beneficial for the treatment of degenerative diseases associated with excess glutamate. Inhibition of GCP II is neuroprotective in a variety of cell and animal models of disease involving excess glutamate. N-acetyl-aspartyl-glutamate can acts as a marker of glutamate carboxypeptidase II inhibition

707124

malfunction

Rattus norvegicus

-

involvement of the endogenous NAAG-NAALADase signaling pathway in cocaine addiction. Inhibition of NAALADase by 2-PMPA attenuates cocaine-induced relapse in rats via a NAAG-mGluR2/3-mediated mechanism, overview

709605

malfunction

Homo sapiens

Q04609

the enzyme is involved in neurological disorders and overexpressed in a number of solid cancers

753551

physiological function

Homo sapiens

-

PSMA acts as a glutamate-preferring carboxypeptidase in human prostate tissue, and plays a role in folic acid utilization and metabolism

710204

physiological function

Arabidopsis thaliana

Q9M1S8

Amp1 mutants display hypersensitivity to abscisic acid, while overexpression of Amp1 causes insensitivity to abscisic acid. Endogenous abscisic acid concentration is increased in Amp1 mutant and decreased in Amp1-overexpressing plants under stress conditions. Application of abscisic acid reduces the Amp1 protein level in plants. Amp1 mutants accumulate excess superoxide and displaye hypersensitivity to oxidative stress. The hypersensitivity of Amp1 mutants to abscisic acid and oxidative stress is partially rescued by reactive oxygen species scavenging agents. Amp1 mutants are tolerant to freezing and drought stress. The abscisic acid hypersensitivity and freezing tolerance of Amp1 mutants are dependent on abscisic acid signaling. Amp1 mutants show elevated soluble sugar content and show hypersensitivity to high concentrations of sugar. The contents of amino acids are changed in Amp1 mutants compared to the wild-type

732580

physiological function

Homo sapiens

Q04609

glutamate carboxypeptidase II has a physiological function in degrading amyloid-beta. Amyloid-beta degradation occurs through S1 pocket but not through S1' pocket responsible for N-acetylaspartylglutamate hydrolysis. Treatment with a S1 pocket-specific chemical inhibitor prevents GCPII from amyloid-beta degradation without any impairment in N-acetylaspartylglutamate hydrolysis. Likewise, specific GCPII inhibitor 2-(phosphonomethyl) pentanedioic acid developed targeting S1' pocket completely blocks the N-acetylaspartylglutamate hydrolysis without any effect on amyloid-beta degradation. Pre-incubation with N-acetylaspartylglutamate and amyloid-beta does not affect amyloid-beta degradation and N-acetylaspartylglutamate hydrolysis, respectively

731253

physiological function

Homo sapiens

Q04609

glutamate carboxypeptidase II is not an amyloid peptide-degrading enzyme

731778

physiological function

Homo sapiens

Q04609

the enzyme participates in glutamate excitotoxicity in the brain

753584