Open AccessCleavage specificity of the serine protease of Aeromonas sobria , a member of the kexin family of subtilases
Author(s) -
Kobayashi Hidetomo,
Takahashi Eizo,
Oguma Keiji,
Fujii Yoshio,
Yamanaka Hiroyasu,
Negishi Tomoe,
ArimotoKobayashi Sakae,
Tsuji Takao,
Okamoto Keinosuke
Publication year - 2006
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2006.00134.x
Subject(s) - furin , serine protease , proteases , cleavage (geology) , subtilisin , protease , serine , kexin , biochemistry , tmprss6 , biology , cleave , chemistry , enzyme , ldl receptor , lipoprotein , paleontology , cholesterol , fracture (geology)
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.