Temperature adaptation of enzymes: A proposed molecular basis for the different catalytic efficiencies of enzymes from ectotherms and endotherms

Philip Low, George N. Somero

Research output: Contribution to journalArticle

46 Scopus citations

Abstract

1. 1. A number of enzymic reactions of ectotherms have lower values for the free energy, the enthalpy and the entropy of activation than the homologous reactions of birds and mammals. 2. 2. Differences in the magnitudes of the activation parameters, which lead to marked differences in the catalytic efficiencies of the homologous enzymes, can be accounted for on the basis of increased weak bond formation during the generation of the activated enzyme-substrate complex in ectothermic systems.

Original languageEnglish (US)
Pages (from-to)307-312
Number of pages6
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume49
Issue number2
DOIs
StatePublished - Oct 15 1974

Keywords

  • activation energy
  • activation thermodynamics
  • d-glyceraldehyde-3-phosphate dehydrogenase
  • glycogen phosphorylase
  • lactate dehydrogenase
  • Temperature
  • temperature adaptation

ASJC Scopus subject areas

  • Medicine(all)

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