Kitagishi K, Hiromi K
J Biochem. 1984 Feb;95(2):529-34. doi: 10.1093/oxfordjournals.jbchem.a134635.
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.
通过稳态抑制动力学分析、荧光滴定和停流法，对嗜热菌蛋白酶（E）与其特异性抑制剂磷酰胺素（N-(α-L-鼠李吡喃糖氧基磷酸)-L-亮氨酰-L-色氨酸）（I）之间的相互作用进行了平衡和动力学研究。通过荧光滴定直接得到的抑制剂常数K1、El复合物的解离常数Kd，以及用停流法得到的表观二级缔合常数kon，与他莫肽的相应常数非常相似（北岸，K.等人（1983年）《生物化学杂志》93卷，47 - 53页和55 - 59页），他莫肽的分子结构与磷酰胺素的不同之处仅在于糖部分C-4原子上OH基团的构型。结果表明，OH基团对于与嗜热菌蛋白酶的结合并非必不可少。
