The Ways of Realization of High Specificity and Efficiency of Enteropeptidase

Title: The Ways of Realization of High Specificity and Efficiency of Enteropeptidase

Volume: 14 Issue: 3

Author(s): Anna G. Mikhailova, Viktoria V. Likhareva, Niels Teich and Lev D. Rumsh

Affiliation:

Keywords: Enteropeptidase, trypsin, trypsinogen, selectivity, substrate analysis

Abstract: Comparative substrate analysis of full-length bovine enteropeptidase and trypsin, bovine and human enteropeptidase light chains was performed using model N-terminal dodecapeptides corresponding to wild-type human trypsinogen and pancreatitis-associated mutant trypsinogens K23R and D22G. The substitution of Lys residue by Arg at P1 leads to 2- fold increase in the efficiency of enteropeptidase hydrolysis; the absence of the negatively charged residue at P2 reduces the efficiency of such hydrolysis by two orders of magnitude. The difference in efficiency of peptide chain hydrolysis after Lys/Arg residues by enteropeptidase compared to trypsin is equal to the difference in hydrolysis by serine proteases of different primary specificity of their specific substrates.

Cite this article as:

Mikhailova G. Anna, Likhareva V. Viktoria, Teich Niels and Rumsh D. Lev, The Ways of Realization of High Specificity and Efficiency of Enteropeptidase, Protein & Peptide Letters 2007; 14 (3) . https://dx.doi.org/10.2174/092986607780090793