Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites

M. Victòria Nogués, Maria Vilanova, Claudi M. Cuchillo

Research output: Contribution to journalReview articleResearchpeer-review

76 Citations (Scopus)

Abstract

Bovine pancreatic ribonuclease A is an enzyme that catalyses the depolymerization of RNA. This process involves the interaction of the enzyme with the alignment on the substrate in the active site and its correct alignment on the surface of the enzyme through multiple binding subsites that essentially recognize the negatively charged phosphate groups of the substrate. The enzyme shows a strong specificity for pyrimidine bases at the 3′-position of the phosphodiester bond that is cleaved and a preference for purine bases at the 5′-position and, probably, for guanine at the next position. On the other hand, the enzyme shows a clear preference for polynucleotide substrates over oligonucleotides. In this review the contributions to the catalytic mechanism of some amino-acid residues that are located at non catalytic binding subsites are analysed. © 1995.
Original languageEnglish
Pages (from-to)16-24
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1253
Issue number1
DOIs
Publication statusPublished - 15 Nov 1995

Keywords

  • Binding sites
  • Catalysis
  • Enzyme kinetics
  • Ribonuclease A
  • Structure

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