Title : Mapping of the active site of glutamate carboxypeptidase II by site-directed mutagenesis.

Pub. Date : 2007 Sep

PMID : 17714508






2 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 To complement and extend the structural studies, we constructed a model of GCPII in complex with its substrate, N-acetyl-l-aspartyl-l-glutamate, which enabled us to predict additional amino acid residues interacting with the bound substrate, and used site-directed mutagenesis to assess the contribution of individual residues for substrate/inhibitor binding and enzymatic activity of GCPII. Ac-Asp-Glu(3-) folate hydrolase 1 Homo sapiens
2 To complement and extend the structural studies, we constructed a model of GCPII in complex with its substrate, N-acetyl-l-aspartyl-l-glutamate, which enabled us to predict additional amino acid residues interacting with the bound substrate, and used site-directed mutagenesis to assess the contribution of individual residues for substrate/inhibitor binding and enzymatic activity of GCPII. Ac-Asp-Glu(3-) folate hydrolase 1 Homo sapiens