Dipeptide synthesis by an aminopeptidase from Streptomyces septatus TH-2 and its application to synthesis of biologically active peptides.
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.
Arima
Jiro
J
Research Institute for Biological Sciences (RIBS), Okayama, 7549-1 Kibichuo-cho, Kaga-gun, Okayama 716-1241, Japan.
Uesugi
Yoshiko
Y
Uraji
Misugi
M
Iwabuchi
Masaki
M
Hatanaka
Tadashi
T
D000626:Aminopeptidases / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D004151:Dipeptides / Q000096:biosynthesis*; D007700:Kinetics; D000432:Methanol / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*; D013816:Thermodynamics
D004151:Dipeptides; D000626:Aminopeptidases; D000432:Methanol