Construction of D-aminoacyl peptides synthetase

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Peptides incorporating D-amino acids are expected to increase the functional variety and applications of peptides. In this study, we constructed the mutant D-aminopeptidases as a convenient tool for synthesis of peptides incorporating D-amino acids. We obtained a serine D-stereospecific amidohydrolase that exhibit peptide bond formation activity by catalysis of aminolysis reaction. The enzyme utilizes D-Pro derivatives as acyl donor substrate, and exhibit efficient synthesis of cyclo (D-Pro-L-Arg) that has chitinase inhibitory activity in a one-pot reaction manner. In addition, we identified the residue, Asn193, which associates the recognition of side chain of acyl donor, from the mutation analysis.