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Peptide synthesis catalysed by Pseudomonas aeruginosa elastase
Author(s) -
Pauchon V.,
Besson C.,
Saulnier J.,
Wallach J.
Publication year - 1993
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1993.tb00241.x
Subject(s) - thermolysin , chemistry , elastase , dipeptide , peptide bond , stereochemistry , peptide synthesis , peptide , amino acid , tyrosine , hydrolysis , biochemistry , enzyme , trypsin
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. aeruginosa elastase permits the synthesis of tyrosine‐containing peptides with tyrosine in the P'1 position. Furthermore, the rates of synthesis for other hydrophobic amino acid amides are higher with elastase than with thermolysin.