EC Number   |
General Information |
Reference |
|---|
   3.4.17.21 | malfunction |
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 |
| 3.4.17.21 | malfunction |
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 |
| 3.4.17.21 | malfunction |
the enzyme is involved in neurological disorders and overexpressed in a number of solid cancers |
753551 |
| 3.4.17.21 | metabolism |
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 |
| 3.4.17.21 | physiological function |
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 |
| 3.4.17.21 | physiological function |
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 |
| 3.4.17.21 | physiological function |
glutamate carboxypeptidase II is not an amyloid peptide-degrading enzyme |
731778 |
| 3.4.17.21 | physiological function |
PSMA acts as a glutamate-preferring carboxypeptidase in human prostate tissue, and plays a role in folic acid utilization and metabolism |
710204 |
| 3.4.17.21 | physiological function |
the enzyme participates in glutamate excitotoxicity in the brain |
753584 |
