Application of linear free energy relationships to the serpin-proteinase inhibition mechanism

Piers Nash, Douglas McFadden, Adrian Whitty

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Linear free energy relationships can be used to link the changes in rate constant for a reaction to changes in the equilibrium caused by alterations in structure. While they have most often been used in the analysis of chemical reactions, they have also been employed to resolve questions in enzymology and protein folding. Here we analyze the reaction of a serpin with a panel of six serine proteinases, and observe that a linear free energy relationship exists between the true second-order rate constant for reaction, k(inh), and the inhibition constant, K(I), indicating that formation of the covalent serpin-enzyme complex may be reversible. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)1-6
Number of pages6
JournalFEBS Letters
Volume475
Issue number1
DOIs
StatePublished - Jun 9 2000
Externally publishedYes

Fingerprint

Serpins
Free energy
Rate constants
Peptide Hydrolases
Protein folding
Protein Folding
Serine Proteases
Chemical reactions
Enzymes

Keywords

  • Inhibition kinetics
  • LFER
  • Poxvirus
  • Protease
  • Proteinaceous inhibitor
  • Structure-activity relationship

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Application of linear free energy relationships to the serpin-proteinase inhibition mechanism. / Nash, Piers; McFadden, Douglas; Whitty, Adrian.

In: FEBS Letters, Vol. 475, No. 1, 09.06.2000, p. 1-6.

Research output: Contribution to journalArticle

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