Peptide synthesis with halophenylalanines by thermolysin

Applied Microbiology and Biotechnology
Y ImaokaA Tanaka

Abstract

Thermolysin was able to catalyze enantioselective peptide synthesis with non-natural amino acids, halophenylalanines. However, the reactivity of thermolysin was considerably influenced by the kind and position of halogen substituents on these analogues. The manner of the recognition of the amino component by the enzyme was different from that of the carboxyl component in the synthesis of peptides with non-natural phenylalanine analogues. The phenomena observed are discussed, based on the kinetic parameters obtained.

Citations

Jul 1, 1997·Journal of Peptide Science : an Official Publication of the European Peptide Society·U EichhornH D Jakubke
Oct 20, 2005·Journal of Bioscience and Bioengineering·M MiyanagaK Nakanishi
Oct 20, 2005·Journal of Bioscience and Bioengineering·M MiyanagaK Nakanishi

Related Concepts

N-(benzyloxycarbonyl)phenylalanylphenylalanine methyl ester, (D-Phe-L-Phe)
Biotechnology
Dipeptides
Endorphenyl
Molecular Stereochemistry
Thermolysin

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