Egmond M R, de Vlieg J
Unilever Research Laboratorium, Olivier van Noortlaan 120, 3133 AT, the, Vlaardingen, Netherlands.
Biochimie. 2000 Nov;82(11):1015-21. doi: 10.1016/s0300-9084(00)01183-4.
Cutinase from Fusarium solani pisi has been studied extensively with respect to its structural and functional properties. The crystal structure of the enzyme was solved to high atomic resolution (1 angstrom), while data on structural dynamics have been obtained from detailed NMR studies. Functional data were mainly derived from kinetic studies using substrate analogues that simplify the kinetic behaviour. The properties of wild-type cutinase are reviewed and discussed in relation with the effects brought about by site-directed variants of the enzyme.
来自豌豆镰孢菌的角质酶在结构和功能特性方面已得到广泛研究。该酶的晶体结构已解析到高原子分辨率(1埃),而关于结构动力学的数据则来自详细的核磁共振研究。功能数据主要来自使用简化动力学行为的底物类似物进行的动力学研究。本文综述并讨论了野生型角质酶的特性以及该酶定点变体所带来的影响。