Binding between thermolysin and its specific inhibitor, phosphoramidon.
Binding between thermolysin and its specific inhibitor, phosphoramidon.
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嗜热菌蛋白酶与其特异性抑制剂磷酰胺之间的结合。
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发表时间：
1984
期刊：
影响因子：
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通讯作者：
K. Hiromi
中科院分区：
文献类型：
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作者：
K. Kitagishi;K. Hiromi
用稳态抑制动力学分析、荧光滴定和停流法研究了嗜热菌蛋白酶（E）与其特异性抑制剂phosphoramidon（I）的相互作用。抑制剂常数K1、通过荧光滴定直接获得的E1复合物的解离常数Kd和用停流法获得的表观二级缔合常数kon与他洛肽的那些非常相似（Kitagishi，K.，等人（1983）J.Biochem.93，47-53和55-59），其分子结构与磷酰胺的不同之处仅在于糖部分的C-4原子处的OH基团的构型。结果表明，OH基团不是与嗜热菌蛋白酶结合所必需的。
Equilibrium and kinetic studies on the interaction between thermolysin (E) and its specific inhibitor (I), phosphoramidon (N-(alpha-L-rhamnopyranosyloxyphospho)-L-leucyl-L-tryptophan), have been made by steady-state inhibitory kinetics analysis, fluorometric titration and the stopped-flow method. The inhibitor constant, K1, the dissociation constant of the El complex, Kd, directly obtained by fluorometric titration, and the apparent second-order association constant, kon, obtained with the stopped-flow method are very similar to those for talopeptin (Kitagishi, K., et al. (1983) J. Biochem. 93, 47-53 and 55-59), whose molecular structure differs from that of phosphoramidon only in the configuration of the OH group at the C-4 atom of the sugar moiety. The result suggested that the OH group is not essential for the binding to thermolysin.