The perfection of substrate-channelling in interacting enzyme systems: Energetics and evolution

Tamás Keleti, Beáta Vértessy, G. Rickey Welch

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Some implications of substrate channelling in interacting enzyme systems are considered, with regard to the energetics and evolution of enzyme action. The transient time, a key analytical parameter relating to the phenomenon of channelling, is the basis of our kinetic study. Bounds on the kinetics of multienzyme complexes are established using (apparent) rate constants emanating from the transient-time formulation of coupled reactions. From a transition state representation of the rate process, it is shown how dynamically and statically organized enzyme systems lead to the modification of current ideas on the evolutionary optimization of the energy profile of enzyme catalysis in situ.

Original languageEnglish
Pages (from-to)75-83
Number of pages9
JournalJournal of Theoretical Biology
Volume135
Issue number1
DOIs
Publication statusPublished - Nov 7 1988

ASJC Scopus subject areas

  • Statistics and Probability
  • Modelling and Simulation
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Agricultural and Biological Sciences(all)
  • Applied Mathematics

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