Flint H J, Whitehead T R, Martin J C, Gasparic A
Rowett Research Institute, Bucksburn, Aberdeen, UK.
Biochim Biophys Acta. 1997 Feb 8;1337(2):161-5. doi: 10.1016/s0167-4838(96)00213-0.
Two xylanases from the rumen anaerobic bacterium Prevotella ruminicola were found to possess highly unusual structures in which family 10 catalytic domains are interrupted by unrelated sequences. XynC from P. ruminicola B(1)4 carries a 160 amino-acid insertion, while a P. ruminicola D31d xylanase carries an unrelated region of 280 amino acids, containing an imperfect 130 amino-acid duplication. Both regions of family 10 similarity were shown to be essential for activity of the D31d enzyme.
研究发现,瘤胃厌氧细菌普氏栖粪杆菌(Prevotella ruminicola)中的两种木聚糖酶具有非常独特的结构,其中10家族催化结构域被不相关的序列打断。普氏栖粪杆菌B(1)4的木聚糖酶C(XynC)带有一个160个氨基酸的插入序列,而普氏栖粪杆菌D31d的一种木聚糖酶带有一个280个氨基酸的不相关区域,其中包含一个130个氨基酸的不完全重复序列。研究表明,10家族相似性的两个区域对于D31d酶的活性都是必不可少的。