二肽基肽酶IV对六肽Met-Ala-Ser-Pro-Phe-Ala的逐步降解
Stepwise degradation of the hexapeptide Met-Ala-Ser-Pro-Phe-Ala by dipeptidyl peptidase IV.
作者信息
Berger E, Fischer G, Neubert K, Barth A
机构信息
Institut für Neurobiologie und Hirnforschung, Akademie der Wissenschaften, Magdeburg, GDR.
出版信息
Biomed Biochim Acta. 1987;46(10):671-6.
Dipeptidyl peptidase IV (dipeptidyl-peptide hydrolase, EC 3.4.14.-) purified from pig kidney was proved to split off the N-terminal dipeptide Met1-Ala2 and, subsequently the dipeptide Ser3-Pro4 from the synthetic model peptide Met-Ala-Ser-Pro-Phe-Ala representing the N-terminal part of a signal sequence of leucocyte interferon. The kinetic parameters for the release of Met1-Ala2 (Km 3.2.10(-5) mol.l-1 and Ser3-Pro4 (Km 1.65.10(-4) mol.l-1, kcat57.9 s-1) were determined. The dipeptides Ser-Pro and Phe-Ala were found to be competitive inhibitors of the hydrolysis of Gly-Pro-NHNp by dipeptidyl peptidase IV.
从猪肾中纯化得到的二肽基肽酶IV（二肽基肽水解酶，EC 3.4.14.-）被证明能够从代表白细胞干扰素信号序列N端部分的合成模型肽Met-Ala-Ser-Pro-Phe-Ala中裂解掉N端二肽Met1-Ala2，随后再裂解掉二肽Ser3-Pro4。测定了释放Met1-Ala2（Km 3.2×10⁻⁵ mol·L⁻¹）和Ser3-Pro4（Km 1.65×10⁻⁴ mol·L⁻¹，kcat 57.9 s⁻¹）的动力学参数。发现二肽Ser-Pro和Phe-Ala是二肽基肽酶IV水解Gly-Pro-NHNp的竞争性抑制剂。
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