Literature summary for 3.4.17.21 extracted from

Ptacek, J.; Nedvedova, J.; Navratil, M.; Havlinova, B.; Konvalinka, J.; Barinka, C.
The calcium-binding site of human glutamate carboxypeptidase II is critical for dimerization, thermal stability, and enzymatic activity (2018), Protein Sci., 27, 1575-1584 .

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General Stability

General Stability	Organism
even a slight disruption of the Ca2+-binding site destabilizes the three-dimensional fold of the enzyme	Homo sapiens

Localization

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	even a slight disruption of the Ca2+-binding site destabilizes the three-dimensional fold of glutamate carboxypeptidase II and is associated with impaired secretion, a high propensity to form nonphysiological oligomers, and an inability to bind active site-targeted ligands. Additionally, the Ca2+-binding site is critical for maintenance of the native homodimeric quaternary arrangement of GCPII, which is indispensable for its enzymatic activity	Homo sapiens
Zn2+	zinc-dependent metallopeptidase	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q04609	-	-

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Release 2023.1 (January 2023)