High-efficiency transpeptidation catalysed by clostripain and electrostatic effects in substrate specificity.
Clostripain catalyses the transpeptidation between benzoylarginin ethyl ester and amino acid amides, oligopeptides, insulin A- and B-chains and tryptic peptides of myoglobin at millimolar substrate concentrations. The reactions proceed with temporary accumulation of the products, followed by hydrolytic decomposition. The yield was not affected significantly by the type of N-terminal amino acid, but was diminished markedly by the negative charges of the amine components. The yields for natural peptides were linearly related to the charge density of the peptides.
Yagisawa
S
S
Faculty of Pharmaceutical Sciences, Nagasaki University, Japan.
Watanabe
S
S
Takaoka
T
T
Azuma
H
H
D000217:Acyltransferases / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D006736:Horses; D007700:Kinetics; D008969:Molecular Sequence Data; D010455:Peptides; D010458:Peptidyl Transferases / Q000378:metabolism*; D013379:Substrate Specificity
D000911:Antibodies, Monoclonal; D010455:Peptides; D000217:Acyltransferases; D010458:Peptidyl Transferases; D003546:Cysteine Endopeptidases; C019913:clostripain