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Literature summary for 3.4.17.21 extracted from

  • Rawlings, N.D.; Barrett, A.J.
    Structure of membrane glutamate carboxypeptidase (1997), Biochim. Biophys. Acta, 1339, 247-252.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
domain structure, sequence alignment with transferrin receptor, the catalytic domain can be assigned to the peptidase family M28 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
male
-

Source Tissue

Source Tissue Comment Organism Textmining
prostate gland
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information hydrolysis of peptide bonds of Asp or Glu to a Glu residue with unsubstituted alpha-carboxyl group. The amide bonds to Glu from the substituted benzoate in folate and methorexate molecules are resistant to hydrolysis Homo sapiens ?
-
?
N-Acetyl-L-Asp-L-Glu + H2O
-
Homo sapiens N-Acetyl-L-Asp + L-Glu
-
?