737745-61-8Relevant articles and documents
Penicillin acylase-catalyzed peptide synthesis: A chemo-enzymatic route to stereoisomers of 3,6-diphenylpiperazine-2,5-dione
Van Langen, Luuk M.,Van Rantwijk, Fred,Svedas, Vytas K.,Sheldon, Roger A.
, p. 1077 - 1083 (2000)
Chiral dipeptides of phenylglycine were synthesized using immobilized Escherichia coli penicillin acylase. The high selectivity of penicillin acylase for L-amino acids as the nucleophile resulted in the efficient acylation of L-phenylglycine by D-phenylglycine amide at pH 9.7 to give D-phenylglycyl-L-phenylglycine in 69% yield. No isomers or tripeptides were formed. The low enantiospecificity of the enzyme for the acyl donor provided the possibility of preparing the corresponding L,L-dipeptides, starting from L-phenylglycine methyl ester as both donor and acceptor at pH 7.5, resulting in a 63% yield of L-phenylglycyl-L-phenylglycine methyl ester. The product precipitated under the reaction conditions; this effectively prevented the formation of oligomers as well as chemical transformation of the product.The dipeptide esters of phenylglycine easily cyclized to diketopiperazines in aqueous methanol. L-Phenylglycyl-L-phenylglycine methyl ester formed L,L-3,6-diphenylpiperazine-2,5-dione (cis); the achiral trans isomer was obtained from D-phenylglycyl-L-phenylglycine methyl ester. Copyright (C) 2000 Elsevier Science Ltd.
