Peptide bond synthesis catalyzed by alpha-chymotrypsin

Journal of Biochemistry
T Oka, K Morihara


alpha-Chymotrypsin [EC] catalyzed the syntheses of peptide bonds with various N-acylated amino acids or peptides having aromatic or hydrophobic amino acid residues at the C-terminal position as carboxyl components, and amino acid derivatives, peptides or their derivatives as amine components. A neutral pH was most efficient and quite high concentrations of alpha-chymotrypsin and starting materials were required for synthesis. Four amine components, hydrophobic or bulky amino acid residues were useful at the N-terminal position. Stereospecificity was also observed at the N-terminal position of amine components. Peptide synthesis was not usually seen when the products were soluble in the reaction mixture. This could be partly overcome by increasing the concentration of either the carboxyl or the amine component to more than ten times that of the other.


Jun 12, 2009·Critical Reviews in Biotechnology·Anshu Gupta, S K Khare
Sep 1, 1982·Applied Biochemistry and Biotechnology·I M ChaikenF Widmer
Feb 1, 1988·International Journal of Peptide and Protein Research·E ChengM Tominaga
Jan 1, 1983·Molecular and Cellular Biochemistry·D Konopińska, F Muzalewski
Apr 15, 2004·Biotechnology and Bioengineering·Iulian M BobeHaruo Ishikawa
Jul 1, 1994·Biotechnology and Bioengineering·S A WilsonK Peek
Sep 1, 2005·Applied Microbiology and Biotechnology·Dinesh Kumar, Tek Chand Bhalla

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