Peptide synthesis catalysed by Pseudomonas aeruginosa elastase.

@article{Pauchon1993PeptideSC,
  title={Peptide synthesis catalysed by Pseudomonas aeruginosa elastase.},
  author={V Pauchon and C{\'e}line Besson and Jo{\"e}lle Saulnier and Joshua Wallach},
  journal={Biotechnology and applied biochemistry},
  year={1993},
  volume={17 ( Pt 2)},
  pages={217-21}
}
Pseudomonas aeruginosa elastase was used for peptide-bond synthesis with benzyloxycarbonylalanine and amino acid amides as nucleophilic substrates. Dipeptide-bond synthesis was observed only for hydrophobic amino acid amides. The rate of peptide synthesis, measured by h.p.l.c., was in the decreasing order: Phe > Leu > Tyr > Val, Ile > Ala, which is consistent with the decreasing order of hydrolysis rates of the corresponding tetrapeptides Ala-Ala-Xaa-Ala. In contrast with thermolysin, Ps… CONTINUE READING