Kobayashi Hidetomo, Takahashi Eizo, Oguma Keiji, Fujii Yoshio, Yamanaka Hiroyasu, Negishi Tomoe, Arimoto-Kobayashi Sakae, Tsuji Takao, Okamoto Keinosuke
Department of Pharmacogenetics, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
FEMS Microbiol Lett. 2006 Mar;256(1):165-70. doi: 10.1111/j.1574-6968.2006.00134.x.
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.
枯草杆菌蛋白酶样蛋白酶已根据催化结构域的序列被分为六个家族。六个家族之一是凯欣家族，其中弗林蛋白酶是一种代表性蛋白酶。凯欣家族的所有成员，除了一个之外，都来自真核生物。唯一的原核生物蛋白酶是嗜水气单胞菌的一种丝氨酸蛋白酶（ASP）。在此，我们基于短肽的切割研究了ASP的底物特异性。结果表明，ASP优先切割两个碱性残基之后的肽键，其中一个是赖氨酸，但不切割单个碱性残基之后的键。这表明ASP催化结构域周围的三级结构与弗林蛋白酶相似，但并不相同。前激肽释放酶被ASP切割成四个片段，这表明该蛋白质必须在特定序列处被切割。
