Guo Haobo, Wlodawer Alexander, Guo Hong
Department of Biochemistry and Cellular and Molecular Biology and Center of Excellence for Structural Biology, University of Tennessee, Knoxville, Tennessee 37996, USA.
J Am Chem Soc. 2005 Nov 16;127(45):15662-3. doi: 10.1021/ja0520565.
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.
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。
