Peptide synthesis catalysed by Pseudomonas aeruginosa elastase.
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.
Pauchon
V
V
Laboratoire de Biochimie Analytique, Université Claude Bernard-Lyon, Villeurbanne, France.
Besson
C
C
Saulnier
J
J
Wallach
J
J
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D002384:Catalysis; D007700:Kinetics; D008969:Molecular Sequence Data; D010196:Pancreatic Elastase / Q000378:metabolism*; D010452:Peptide Biosynthesis; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D000596:Amino Acids; D010196:Pancreatic Elastase