Dipeptide synthesis by an aminopeptidase from Streptomyces septatus TH-2 and its application to synthesis of biologically active peptides
Dipeptide synthesis by an aminopeptidase from Streptomyces septatus TH-2 and its application to synthesis of biologically active peptides
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DOI：
10.1128/aem.00150-06
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发表时间：
2006-06-01
影响因子：
4.4
通讯作者：
Hatanaka, Tadashi
中科院分区：
文献类型：
--
作者：
Arima, Jiro;Uesugi, Yoshiko;Hatanaka, Tadashi
以98%甲醇为溶剂，以游离氨基酸为酰基供体，氨基酰甲酯为酰基受体，研究了隔链霉菌TH-2氨基肽酶(SSAP)合成二肽的反应条件。在98%的甲醇中，SSAP在100h以上仍保持其活性，在苯丙氨基-苯丙氨酸甲酯的合成中，当超过50%的游离苯丙氨酸转化为产物时，酶反应达到平衡。在研究SSAP对酰基供体和酰基受体的特异性时，SSAP对各种游离氨基酸和氨基酰甲酯表现出广泛的特异性。此外，我们还将SSAP应用于天冬氨酸苯丙氨酸、丙氨酰-酪氨酸和丙氨酰-酪氨酸甲酯等生物活性多肽的合成。
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.