Siezen R J, Leunissen J A
Department of Biophysical Chemistry, NIZO, Ede, The Netherlands.
Protein Sci. 1997 Mar;6(3):501-23. doi: 10.1002/pro.5560060301.
Subtilases are members of the clan (or superfamily) of subtilisin-like serine proteases. Over 200 subtilases are presently known, more than 170 of which with their complete amino acid sequence. In this update of our previous overview (Siezen RJ, de Vos WM, Leunissen JAM, Dijkstra BW, 1991, Protein Eng 4:719-731), details of more than 100 new subtilases discovered in the past five years are summarized, and amino acid sequences of their catalytic domains are compared in a multiple sequence alignment. Based on sequence homology, a subdivision into six families is proposed. Highly conserved residues of the catalytic domain are identified, as are large or unusual deletions and insertions. Predictions have been updated for Ca(2+)-binding sites, disulfide bonds, and substrate specificity, based on both sequence alignment and three-dimensional homology modeling.
枯草杆菌蛋白酶属于枯草杆菌蛋白酶样丝氨酸蛋白酶家族（或超家族）。目前已知超过200种枯草杆菌蛋白酶，其中170多种具有完整的氨基酸序列。在本次对我们之前综述（Siezen RJ、de Vos WM、Leunissen JAM、Dijkstra BW，1991年，《蛋白质工程》4：719 - 731）的更新中，总结了过去五年中发现的100多种新枯草杆菌蛋白酶的详细信息，并在多序列比对中比较了它们催化结构域的氨基酸序列。基于序列同源性，提出了分为六个家族的分类方法。确定了催化结构域的高度保守残基，以及大的或不寻常的缺失和插入。基于序列比对和三维同源建模，更新了对钙结合位点、二硫键和底物特异性的预测。
