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Literature summary for 3.4.17.21 extracted from

  • Navratil, M.; Tykvart, J.; Schimer, J.; Pachl, P.; Navratil, V.; Rokob, T.; Hlouchova, K.; Rulisek, L.; Konvalinka, J.
    Comparison of human glutamate carboxypeptidases II and III reveals their divergent substrate specificities (2016), FEBS J., 283, 2528-2545 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray structure of the inactive enzyme with the engineered mutation E424A in complex with beta-citrylglutamate, hanging drop vapour diffusion method Homo sapiens

Protein Variants

Protein Variants Comment Organism
E424A inactive mutant enzyme Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no modulation of activity by divalent cations Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q04609
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no cleavage of beta-citrylglutamate Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
GCPII
-
Homo sapiens
glutamate carboxypeptidase II
-
Homo sapiens
Prostate-specific membrane antigen
-
Homo sapiens
PSMA
-
Homo sapiens

General Information

General Information Comment Organism
malfunction the enzyme is involved in neurological disorders and overexpressed in a number of solid cancers Homo sapiens