Article
Ala657 and conserved active site residues promote fibroblast activation protein endopeptidase activity via distinct mechanisms of transition state stabilization.
Biochemistry - 17 Apr 2007
Meadows Sarah A, Edosada Conrad Yap, Mayeda Mark, Tran Thuy, Quan Clifford, Raab Helga, Wiesmann Christian, Wolf Beni B
Abstract excerpt
Fibroblast activation protein (FAP) and dipeptidyl peptidase-4 (DPP-4) are highly homologous serine proteases of the prolyl peptidase family and therapeutic targets for cancer and diabetes, respectively. Both proteases display dipeptidyl peptidase activity, but FAP alone has endopeptidase activity. FAP Ala657, which corresponds to DPP-4 Asp663, is important for endopeptidase activity; however, its specific role...
Topics
- Alanine
- Antigens, Neoplasm
- Binding Sites
- Biomarkers, Tumor
- Cell Line
- Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
- Endopeptidases
- Gelatinases
- Humans
- Membrane Proteins
- Models, Molecular
- Molecular Structure
- Mutagenesis, Site-Directed