Temperature Adaptation of Enzymes: Roles of the Free Energy, the Enthalpy, and the Entropy of Activation
- 1 February 1973
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 70 (2), 430-432
- https://doi.org/10.1073/pnas.70.2.430
Abstract
The enzymic reactions of ectothermic (cold-blooded) species differ from those of avian and mammalian species in terms of the magnitudes of the three thermodynamic activation parameters, the free energy of activation (DeltaG()), the enthalpy of activation (DeltaH()), and the entropy of activation (DeltaS()). Ectothermic enzymes are more efficient than the homologous enzymes of birds and mammals in reducing the DeltaG() "energy barrier" to a chemical reaction. Moreover, the relative importance of the enthalpic and entropic contributions to DeltaG() differs between these two broad classes of organisms.Keywords
This publication has 8 references indexed in Scilit:
- Conformational changes in rabbit muscle aldolase. Kinetic studiesBiochemistry, 1970
- Structural and catalytic properties of lobster muscle glycogen phosphorylase.1969
- Glyceraldehyde 3-Phosphate Dehydrogenase from Pig MuscleNature, 1968
- The Catalytic and Regulatory Properties of EnzymesAnnual Review of Biochemistry, 1968
- STRUCTURAL AND FUNCTIONAL PROPERTIES OF THE H AND M SUBUNITS OF LACTIC DEHYDROGENASES*Annals of the New York Academy of Sciences, 1965
- COMPARATIVE ENZYMOLOGY OF LACTIC DEHYDROGENASES .4. FUNCTION OF SULFHYDRYL GROUPS IN LACTIC DEHYDROGENASES AND SEQUENCE AROUND ESSENTIAL GROUP1965
- Structure and Catalytic Activity of Alcohol DehydrogenasesNature, 1964