EVOLUTIONARY DIVERGENCE AND CONSERVATION OF TRYPSIN
EVOLUTIONARY DIVERGENCE AND CONSERVATION OF TRYPSIN
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DOI：
10.1093/protein/7.1.57
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发表时间：
1994-01-01
期刊：
影响因子：
--
通讯作者：
WILSON, KS
中科院分区：
文献类型：
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作者：
RYPNIEWSKI, WR;PERRAKIS, A;WILSON, KS
收集了数据库中现有的胰蛋白酶序列，首先使用氨基酸序列同源性进行比对，然后使用奶牛、灰色链霉菌和尖孢镰刀菌胰蛋白酶的叠加晶体结构进行比对。根据这种多重定位构建的系统发育树与胰蛋白酶从原核生物和真核生物的共同祖先持续进化分化相一致。晶体结构的比较揭示了二级结构的严格守恒。同样，在所有序列的比对中，插入和删除只发生在已知晶体结构中二级结构元素之间环路对应的区域。保守残基聚集在活性位点周围。几乎所有的保守残基都与蛋白的一个基本功能特征有关：酶原活化、催化和底物特异性。相反，蛋白质疏水核心和钙离子结合位点的残基通常不保守。详细讨论了胰蛋白酶的保守性及其性质。
The trypsin sequences currently available in the data banks have been collected and aligned using first the amino acid sequence homology and, subsequently, the superposed crystal structures of trypsins from the cow, the bacterium Streptomyces griseus and the fungus Fusarium oxysporum. The phylogenetic tree constructed according to this multiple alignment is consistent with a continuous evolutionary divergence of trypsin from a common ancestor of both prokaryotes and eukaryotes. Comparison of crystal structures reveals a strict conservation of secondary structure. Similarly, in the alignment of all the sequences, insertions and deletions occur only in regions corresponding to loops between the secondary structure elements in the known crystal structures. The conserved residues cluster around the active site. Almost all conserved residues can be associated with one of the basic functional features of the protein: zymogen activation, catalysis and substrate specificity. In contrast, the residues of the hydrophobic core of the protein and the calcium ion binding sites are generally not conserved. The conserved features of trypsin and the nature of the conservation are discussed in detail.