Peptide synthesis with halophenylalanines by thermolysin.
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.
Imaoka
Y
Y
Department of Synthetic Chemistry and Biological Chemistry, Faculty of Engineering, Kyoto University, Japan.
Kawamoto
T
T
Ueda
M
M
Tanaka
A
A
D000595:Amino Acid Sequence; D001709:Biotechnology; D004151:Dipeptides / Q000138:chemical synthesis* / Q000737:chemistry; D007700:Kinetics; D015394:Molecular Structure; D010649:Phenylalanine / Q000031:analogs & derivatives; D013237:Stereoisomerism; D013820:Thermolysin
D004151:Dipeptides; D010649:Phenylalanine; C051209:N-(benzyloxycarbonyl)phenylalanylphenylalanine methyl ester; D013820:Thermolysin