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. 2000 Sep 15;350(Pt 3):671–676.

Function of the N-terminal propeptide of an aminopeptidase from Vibrio proteolyticus.

Z Z Zhang 1, S Nirasawa 1, Y Nakajima 1, M Yoshida 1, K Hayashi 1
PMCID: PMC1221296  PMID: 10970778

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 (k(cat) and K(m)) 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.

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Selected References

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