Involvement of the Arg566 residue of Aeromonas sobria serine protease in substrate specificity

Aeromonas sobria serine protease (ASP) is an extracellular serine protease secreted by the organism. Here, we identified the amino acid residue of ASP that contributes to substrate specificity by using both synthetic peptides and biological protein components. The results showed that the arginine re...

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Veröffentlicht in:	PloS one 2017-10, Vol.12 (10), p.e0186392-e0186392
Hauptverfasser:	Kobayashi, Hidetomo, Otsubo, Tadamune, Teraoka, Fumiteru, Ikeda, Kiyoshi, Seike, Soshi, Takahashi, Eizo, Okamoto, Keinosuke, Yoshida, Toru, Tsuge, Hideaki, Yamanaka, Hiroyasu
Format:	Artikel
Sprache:	eng
Schlagworte:	Acids Aeromonas Aeromonas - enzymology Aeromonas hydrophila Amino Acid Sequence Amino acids Arginine Arginine - chemistry Arginine - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological effects Biology and Life Sciences Catalysis Cholera Collaboration Environmental science Fibrinogen - metabolism Humans Infectious diseases Kininogens - metabolism Laboratories Life sciences Molecular Chaperones - metabolism Mutagenesis Mutagenesis, Site-Directed Mutation Organic chemistry Peptides Pharmaceutical sciences Point mutation Protease Proteins Proteolysis Research and Analysis Methods Sepsis Serine Serine Proteases - chemistry Serine Proteases - genetics Serine Proteases - metabolism Serine proteinase Substrate Specificity Substrates Synthetic peptides Vibrio cholerae
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