Maruyama S, Miyoshi S, Nomura G, Suzuki M, Tanaka H, Maeda H
Fermentation Research Institute, Agency of Industrial Science and Technology, Ibaraki, Japan.
Biochim Biophys Acta. 1993 Mar 5;1162(1-2):72-6. doi: 10.1016/0167-4838(93)90129-f.
A proline-specific dipeptidylcarboxypeptidase, which removes diproline from the C-terminus of the proline-containing peptides, such as Boc-Pro-Pro-Pro-Pro and Leu-Pro-Pro-Pro-Pro-Pro, has recently been purified from a Streptomyces sp. The specificity of the enzyme for various imino acid-containing synthetic peptide substrates was further studied. The peptides with proline, hydroxyproline, or dehydroproline at the P2' position were found to be good substrates, while those with pipecolic acid, D-proline or other usual amino acids at the P2' position were scarcely hydrolyzed. The peptides with proline, dehydroproline, pipecolic acid, or N-methyl-alanine at the P1' position were well-hydrolyzed, while those with hydroxyproline or D-proline at the P1' position were not hydrolyzed. Utilizing this high specificity for imino acids, Boc-Pro-Pro-Pro-Pro was synthesized by the enzyme using Boc-Pro-Pro as the acidic component and Pro-Pro as the basic component.
一种脯氨酸特异性二肽基羧肽酶，可从含脯氨酸的肽的C末端去除二脯氨酸，如Boc-Pro-Pro-Pro-Pro和Leu-Pro-Pro-Pro-Pro-Pro，最近已从链霉菌属中纯化出来。进一步研究了该酶对各种含亚氨基酸的合成肽底物的特异性。发现在P2'位置含有脯氨酸、羟脯氨酸或脱氢脯氨酸的肽是良好的底物，而在P2'位置含有哌啶酸、D-脯氨酸或其他常见氨基酸的肽几乎不被水解。在P1'位置含有脯氨酸、脱氢脯氨酸、哌啶酸或N-甲基丙氨酸的肽能被很好地水解，而在P1'位置含有羟脯氨酸或D-脯氨酸的肽则不被水解。利用这种对亚氨基酸的高特异性，该酶以Boc-Pro-Pro作为酸性成分和Pro-Pro作为碱性成分合成了Boc-Pro-Pro-Pro-Pro。
