ABSTRACTThe synthesis of diversedl-configuration dipeptides in a one-pot reaction was demonstrated by using a function of the aminolysis reaction of ad-stereospecific amidohydrolase fromStreptomycessp., a clan SE, S12 family peptidase categorized as a peptidase withd-stereospecificity. The enzyme was able to use various aminoacyl derivatives, includingl-aminoacyl derivatives, as acyl donors and acceptors. Investigations of the specificity of the peptide synthetic activity revealed that the enzyme preferentially usedd-aminoacyl derivatives as acyl donors. In contrast,l-amino acids and their derivatives were preferentially used as acyl acceptors. Consequently, the synthesized dipeptides had adl-configuration whend- andl-aminoacyl derivatives were mixed in a one-pot reaction. This report also describes that the enzyme produced cyclo(d–Pro-l-Arg), a specific inhibitor of family 18 chitinase, with a conversion rate ford-Pro benzyl ester andl-Arg methyl ester to cyclo(d-Pro–l-Arg) of greater than 65%. Furthermore, based on results of cyclo(d-Pro–l-Arg) synthesis, we propose a reaction mechanism for cyclo(d-Pro–l-Arg) production.
Factors governing helical preference of peptides containing multiple alpha,alpha-dialkyl amino acids.
