Convergent dynamics in the protease enzymatic superfamily

Vincenzo Carnevale, Simone Raugei, Cristian Micheletti, Paolo Carloni

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

Proteases regulate various aspects of the life cycle in all organisms by cleaving specific peptide bonds. Their action is so central for biochemical processes that at least 2% of any known genome encodes for proteolytic enzymes. Here we show that selected proteases pairs, despite differences in oligomeric state, catalytic residues, and fold, share a common structural organization of functionally relevant regions which are further shown to undergo similar concerted movements. The structural and dynamical similarities found pervasively across evolutionary distant clans point to common mechanisms for peptide hydrolysis.

Original languageEnglish
Pages (from-to)9766-9772
Number of pages7
JournalJournal of the American Chemical Society
Volume128
Issue number30
DOIs
Publication statusPublished - Aug 2 2006

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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