Mutation in the substrate-binding site of aminopeptidase B confers new enzymatic properties.

@article{Pham2011MutationIT,
  title={Mutation in the substrate-binding site of aminopeptidase B confers new enzymatic properties.},
  author={Viet-La{\"i} Pham and C{\'e}cile Gouzy-Darmon and Julien Pernier and Chantal Hanquez and Vivian Hook and Margery C. Beinfeld and Pierre Nicolas and Catherine Etchebest and Thierry Foulon and Sandrine Cadel},
  journal={Biochimie},
  year={2011},
  volume={93 4},
  pages={730-41}
}
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, GXMEN (potential substrate binding site) and HEXXHX(18)E (Zn(2+)-binding site). In… CONTINUE READING