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- W4247382811 abstract "An aminopeptidase from Vibrio proteolyticus was translated as a preproprotein consisting of four domains: a signal peptide, an N-terminal propeptide, a mature region and a C-terminal propeptide. Protein expression and analysis of the activity results demonstrated that the N-terminal propeptide was essential to the formation of the active enzyme in Escherichia coli. Urea dissolution of inclusion bodies and dialysis indicated that the N-terminal propeptide could facilitate the correct folding of the enzyme in vitro. Using l-Leu-p-nitroanilide as the substrate, the kinetic parameters (kcat and Km) of the pro-aminopeptidase and processed aminopeptidases were analysed. The results suggested that the N-terminal propeptide inhibited enzyme activity of the mature region. In contrast, the C-terminal propeptide did not show evidence of forming an active enzyme, of correctly folding in vitro or of inhibiting the active region." @default.
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- W4247382811 date "2000-09-15" @default.
- W4247382811 modified "2023-09-26" @default.
- W4247382811 title "Function of the N-terminal propeptide of an aminopeptidase from Vibrio proteolyticus" @default.
- W4247382811 doi "https://doi.org/10.1042/0264-6021:3500671" @default.
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