Cygler M, Schrag J D, Sussman J L, Harel M, Silman I, Gentry M K, Doctor B P
Biotechnology Research Institute, National Research Council of Canada, Montréal, Québec.
Protein Sci. 1993 Mar;2(3):366-82. doi: 10.1002/pro.5560020309.
Based on the recently determined X-ray structures of Torpedo californica acetylcholinesterase and Geotrichum candidum lipase and on their three-dimensional superposition, an improved alignment of a collection of 32 related amino acid sequences of other esterases, lipases, and related proteins was obtained. On the basis of this alignment, 24 residues are found to be invariant in 29 sequences of hydrolytic enzymes, and an additional 49 are well conserved. The conservation in the three remaining sequences is somewhat lower. The conserved residues include the active site, disulfide bridges, salt bridges, and residues in the core of the proteins. Most invariant residues are located at the edges of secondary structural elements. A clear structural basis for the preservation of many of these residues can be determined from comparison of the two X-ray structures.
基于近期测定的加州电鳐乙酰胆碱酯酶和白地霉脂肪酶的X射线结构及其三维叠加，得到了一组32个其他酯酶、脂肪酶及相关蛋白质的相关氨基酸序列的改进比对。基于此比对，发现在29个水解酶序列中有24个残基是不变的，另有49个残基高度保守。其余三个序列中的保守性略低。保守残基包括活性位点、二硫键、盐桥以及蛋白质核心中的残基。大多数不变残基位于二级结构元件的边缘。通过比较这两个X射线结构，可以确定许多这些残基得以保留的明确结构基础。
