Literature summary for 3.4.17.21 extracted from

Lee, S.; Kim, H.; Cheong, Y.; Kim, M.; Jo, S.; Youn, H.; Park, S.
S1 pocket of glutamate carboxypeptidase II: A new binding site for amyloid-beta degradation (2013), Biochem. Biophys. Res. Commun., 438, 765-771.

Search for more literature for 3.4.17.21

Cloned(Commentary)

Cloned (Comment)	Organism
expression in PC3 cell	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
2-(phosphonomethyl) pentanedioic acid	inhibitor completely blocks N-acetylaspartylglutamate cleavage activity but not Amyloid-beta degradation	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q04609	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
U-87MG cell	-	Homo sapiens	-

General Information

General Information	Comment	Organism
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	Homo sapiens

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Release 2023.1 (January 2023)