Cleavage specificity of the serine protease of Aeromonas sobria, a member of the kexin family of subtilases
Cleavage specificity of the serine protease of Aeromonas sobria, a member of the kexin family of subtilases
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DOI：
10.1111/j.1574-6968.2006.00134.x
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发表时间：
2006-03-01
影响因子：
2.1
通讯作者：
Okamoto, K
中科院分区：
文献类型：
--
作者：
Kobayashi, H;Takahashi, E;Okamoto, K
枯草杆菌蛋白酶样蛋白酶已被分为六个家族的基础上的催化结构域的序列。这六种蛋白酶之一是kexin家族，弗林蛋白酶是其中的代表性蛋白酶。克新家族的所有成员，除了一个，都来自真核生物。一种原核蛋白酶是温和气单胞菌（ASP）的丝氨酸蛋白酶。在这里，我们研究了基于短肽裂解的ASP的底物特异性。结果表明，ASP优先切割两个碱性残基（其中一个为Lys）后的肽键，而不切割单个碱性残基后的肽键。这表明ASP催化结构域周围的三级结构与弗林蛋白酶类似，但不相同。前激肽释放酶被ASP切割成四个片段，表明该蛋白质必须在特定序列处被切割。
Subtilisin-like proteases have been grouped into six families based on a sequence of the catalytic domain. One of the six is the kexin family, of which furin is a representative protease. All members of the kexin family, except one, are from eukaryotes. The one prokaryotic protease is a serine protease of Aeromonas sorbria (ASP). Here, we examined the substrate specificity of ASP based on the cleavage of short peptides. The results showed that ASP preferentially cleaves the peptide bond following two basic residues, one of which is Lys, but not the bond following a single basic residue. This indicates that the tertiary structure around the catalytic domain of ASP resembles, but is not identical to that of furin. Prekallikrein was cleaved into four fragments by ASP, indicating that the protein must be cleaved at specific sequences.