Inhibition of Serine Proteinases Belonging to the Chymotrypsin Superfamily by the Cyclic Thiolic Compound YS3025: A Comparative Crystallographic Study

K. D. Carugo, M. Rizzi, M. Fasano, M. Luisetti, C. Larosa, P. Ascenzi, M. Bolognesi

Research output: Contribution to journalArticle

Abstract

The synthetic cyclic thiolic compound 3-[2-(2-thiophencarboxythio)]-propanoyl-4-thiazolidin carboxylic acid (YS3025) acts as an effective inhibitor of bovine α-chymotrypsin. In the present communication YS3025 binding studies are extended to bovine β-trypsin and porcine pancreatic elastase, by means of crystallographic difference Fourier techniques. For all the enzymes considered, the thiophencarbonyl moiety of YS3025 is located at the entrance of the inhibited proteinase primary specificity pocket (S1), covalently linked to the catalytic Ser195 OG atom, and forming an acyl-enzyme complex. These observations allow to select between alternative binding (and inhibition) mechanisms for YS3025 and related molecules to serine proteinases belonging to the chymotrypsin superfamily.

Original languageEnglish
Pages (from-to)32-39
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume193
Issue number1
DOIs
Publication statusPublished - May 28 1993

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

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