The ways of realization of high specificity and efficiency of enteropeptidase.
The ways of realization of high specificity and efficiency of enteropeptidase.
复制标题
肠肽酶高特异性、高效率的实现途径
DOI：
10.2174/092986607780090793
复制
发表时间：
2007
影响因子：
1.6
通讯作者：
L. Rumsh
中科院分区：
文献类型：
--
作者：
A. G. Mikhailova;V. V. Likhareva;N. Teich;L. Rumsh
使用对应于野生型人胰蛋白酶原和胰腺炎相关突变型胰蛋白酶原K23 R和D22 G的N-末端十二肽模型，对全长牛肠肽酶和胰蛋白酶、牛和人肠肽酶轻链进行比较底物分析。在P1处用Arg取代Lys残基导致肠肽酶水解效率增加2倍;在P2处不存在带负电荷的残基使这种水解的效率降低两个数量级。与胰蛋白酶相比，肠肽酶在Lys/Arg残基后的肽链水解效率的差异等于丝氨酸蛋白酶对其特异性底物的不同主要特异性的水解差异。
Comparative substrate analysis of full-length bovine enteropeptidase and trypsin, bovine and human enteropeptidase light chains was performed using model N-terminal dodecapeptides corresponding to wild-type human trypsinogen and pancreatitis-associated mutant trypsinogens K23R and D22G. The substitution of Lys residue by Arg at P1 leads to 2-fold increase in the efficiency of enteropeptidase hydrolysis; the absence of the negatively charged residue at P2 reduces the efficiency of such hydrolysis by two orders of magnitude. The difference in efficiency of peptide chain hydrolysis after Lys/Arg residues by enteropeptidase compared to trypsin is equal to the difference in hydrolysis by serine proteases of different primary specificity of their specific substrates.