Preliminary crystallographic characterization of BSAP, an extracellular aminopeptidase from Bacillus subtilis.

@article{Reiland2004PreliminaryCC,
  title={Preliminary crystallographic characterization of BSAP, an extracellular aminopeptidase from Bacillus subtilis.},
  author={Vera Reiland and Yifat Fundoiano-Hershcovitz and Gali Golan and Rotem Gilboa and Yuval Shoham and G. Shoham},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2004},
  volume={60 Pt 12 Pt 2},
  pages={2371-6}
}
The extracellular aminopeptidase from Bacillus subtilis (BSAP) has recently been cloned, overexpressed and purified from Escherichia coli. It is a monomer with a molecular weight of 46 425 Da, consisting of 425 amino-acid residues and a double-zinc catalytic centre. The recombinant enzyme was found to be stable for 20 min at 353 K, to function optimally in the pH range 8-9 and to prefer basic and large hydrophobic N-terminal amino acids in peptide and protein substrates. As such, this enzyme… CONTINUE READING