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• W2140247756 abstract "ABSTRACT Dipeptide synthesis by aminopeptidase from Streptomyces septatus TH-2 (SSAP) was demonstrated using free amino acid as an acyl donor and aminoacyl methyl ester as an acyl acceptor in 98% methanol (MeOH). SSAP retained its activity after more than 100 h in 98% MeOH, and in the case of phenylalanyl-phenylalanine methyl ester synthesis, the enzyme reaction reached equilibrium when more than 50% of the free phenylalanine was converted to the product. In an investigation of the specificity of SSAP toward acyl donors and acyl acceptors, SSAP showed a broad specificity toward various free amino acids and aminoacyl methyl esters. Furthermore, we applied SSAP to the synthesis of several biologically active peptides, such as aspartyl-phenylalanine, alanyl-tyrosine, and valyl-tyrosine methyl esters." @default.
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• W2140247756 date "2006-06-01" @default.
• W2140247756 modified "2023-09-29" @default.
• W2140247756 title "Dipeptide Synthesis by an Aminopeptidase from <i>Streptomyces septatus</i> TH-2 and Its Application to Synthesis of Biologically Active Peptides" @default.
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• W2140247756 doi "https://doi.org/10.1128/aem.00150-06" @default.
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