Literature summary for 3.4.17.21 extracted from

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

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Inhibitors

Inhibitors	Comment	Organism	Structure
2-(phosphonomethyl)pentanedioic acid	completely blocks the NAAG hydrolysis without any effect on amyloid-beta degradation	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q04609	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
amyloid-beta + H2O	the enzyme has two distinctive binding sites for two different substrates. Amyloid-beta degradation occurs through S1 pocket but not through S1' pocket responsible for hydrolysis of N-acetyl-L-aspartyl-L-glutamate. Pre-incubation with N-acetyl-L-aspartyl-L-glutamate and amyloid-beta does not affect amyloid-beta degradation and hydrolysis of N-acetyl-L-aspartyl-L-glutamate, respectively	Homo sapiens	?	-	?
N-acetyl-L-aspartyl-L-glutamate + H2O	-	Homo sapiens	N-acetyl-L-Asp + L-Glu	-	?

Synonyms

Synonyms	Comment	Organism
GCPII	-	Homo sapiens
glutamate carboxypeptidase II	-	Homo sapiens

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Release 2023.1 (January 2023)