丝氨酸羧基肽酶中四面体加合物稳定化的一般酸碱机制：一项计算研究。
A general acid-base mechanism for the stabilization of a tetrahedral adduct in a serine-carboxyl peptidase: a computational study.
作者信息
Guo Haobo, Wlodawer Alexander, Guo Hong
机构信息
Department of Biochemistry and Cellular and Molecular Biology and Center of Excellence for Structural Biology, University of Tennessee, Knoxville, Tennessee 37996, USA.
出版信息
J Am Chem Soc. 2005 Nov 16;127(45):15662-3. doi: 10.1021/ja0520565.
PMID:16277482
Abstract
The QM/MM MD and free energy simulations show that serine-carboxyl peptidases (sedolisins) may stabilize the tetrahedral intermediates and tetrahedral adducts primarily through a general acid-base mechanism involving Asp (Asp164 for kumamolisin-As) rather than the oxyanion-hole interactions as in the cases of serine proteases.
摘要
量子力学/分子力学分子动力学（QM/MM MD）和自由能模拟表明，丝氨酸羧肽酶（sedolisins）可能主要通过涉及天冬氨酸（对于嗜热栖热放线菌丝氨酸羧肽酶As来说是天冬氨酸164）的一般酸碱机制来稳定四面体中间体和四面体加合物，而不是像丝氨酸蛋白酶那样通过氧负离子洞相互作用。
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