Remarkable phylum selectivity of a Schistocerca gregaria trypsin inhibitor: The possible role of enzyme-inhibitor flexibility

A. Patthy, S. Amir, Z. Malik, Á Bódi, J. Kardos, B. Asbóth, L. Gráf

Research output: Contribution to journalArticle

31 Citations (Scopus)


A 35-mer polypeptide isolated from the hemolymph of desert locust Schistocerca gregaria (SG) proved to be a canonical inhibitor of bovine trypsin (Ki = 0.2 μM). Despite having a trypsin-specific arginine at the primary specificity P1 site, it inhibits bovine chymotrypsin almost as well (Ki = 2 μM). Furthermore, while the latter reactivity improves 104-fold by the single replacement of P1 Arg by Leu, changing P1 from Lys to Met only moderately improves trypsin affinity (Ki = 30 nM). The apparent low compatibility to trypsin, however, is not observed vs two arthropodal trypsins: SG peptides with P1 Arg inhibit crayfish and shrimp trypsins with Ki values in the picomolar range. This unprecedented high discrimination between orthologous enzymes is postulated to derive from flexibility differences in the protein-protein interaction. The more than four orders of magnitude phylum selectivity makes these peptides prospective candidates for agricultural use.

Original languageEnglish
Pages (from-to)179-187
Number of pages9
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - Feb 15 2002



  • Conformational flexibility
  • Endogenous inhibitors
  • FT-IR
  • Hydrogen exchange
  • Insecticides
  • Orthologous enzymes
  • Serine proteases

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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