Literature summary for 3.4.17.21 extracted from

Naushad, S.M.; Janaki Ramaiah, M.; Stanley, B.A.; Prasanna Lakshmi, S.; Vishnu Priya, J.; Hussain, T.; Alrokayan, S.A.; Kutala, V.K.
In silico approaches to identify the potential inhibitors of glutamate carboxypeptidase II (GCPII) for neuroprotection (2016), J. Theor. Biol., 406, 137-142 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	pharmacophore analysis followed by QSAR studies proposes a N-acetyl aspartyl glutamate-analogue as the most potent inhibitor of the enzyme, effective across all the genetic variants of glutamate carboxypeptidase II. This molecule satisfies Lipinski rule of five and rule of three for drug-likeliness. Being a N-acetyl aspartyl glutamate-analogue, this molecule might confer neuroprotection by inhibiting glutamatergic neurotransmission mediated by N-acetylated alpha-linked acidic dipeptidase (NAALADase), a splice variant of glutamate carboxypeptidase II	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	membrane-bound	Homo sapiens	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	zinc metallo-enzyme, contains two zinc ions co-ordinated by side chain of His377, Asp387, Glu425, Asp453, His553, which are indispensable for hydrolytic activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q04609	-	-

Synonyms

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

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Release 2023.1 (January 2023)