Article
Mutation in the substrate-binding site of aminopeptidase B confers new enzymatic properties.
Biochimie - 1 Apr 2011
Pham Viet-Laï, Gouzy-Darmon Cécile, Pernier Julien, Hanquez Chantal, Hook Vivian, Beinfeld Margery C, Nicolas Pierre, Etchebest Catherine, Foulon Thierry, Cadel Sandrine
Abstract excerpt
Aminopeptidase B (Ap-B) catalyzes the cleavage of arginine and lysine residues at the N-terminus of various peptide substrates. In vivo, it participates notably in the miniglucagon and cholecystokinin 8 processing, but the complete range of physiological functions of Ap-B remains to be discovered. Ap-B is a member of the M1 family of Zn(2+)-metallopeptidases that are characterized by two highly conserved motives,...
Topics
- Amino Acid Motifs
- Aminopeptidases
- Animals
- Binding Sites
- Catalytic Domain
- Cattle
- Metalloproteases
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation
- Protein Stability
- Rats
- Substrate Specificity