Enthalpy-entropy compensation and the isokinetic temperature in enzyme catalysis.

Publisher: Springer India, in co-publication with Indian Academy of Sciences Country of Publication: India NLM ID: 8100809 Publication Model: Print Cited Medium: Internet ISSN: 0973-7138 (Electronic) Linking ISSN: 02505991 NLM ISO Abbreviation: J Biosci Subsets: MEDLINE

Publication: <2006- >: New Delhi : Springer India, in co-publication with Indian Academy of Sciences
Original Publication: [Bangalore] : Indian Academy of Sciences, 1979-

Adenosine Triphosphatases/*metabolism ; Enzyme Assays/*statistics & numerical data ; Fish Proteins/*metabolism; Animals ; Biocatalysis ; Data Interpretation, Statistical ; Fishes/metabolism ; Kinetics ; Temperature ; Thermodynamics

Enthalpy-entropy compensation supposes that differences in activation enthalpy ΔH++ for different reactions (or, typically in biochemistry, the same reaction catalysed by enzymes obtained from different species) may be compensated for by differences in activation entropy ΔS++. At the isokinetic temperature the compensation is exact, so that all samples have the same activity. These ideas have been controversial for several decades, but examples are still frequently reported as evidence of a real phenomenon, nearly all of the reports ignoring or discounting the possibility of a statistical artefact. Even for measurements in pure chemistry artefacts occur often, and they are almost inescapable in enzyme kinetics and other fields that involve biological macromolecules, on account of limited stability and the fact that kinetic equations are normally valid only over a restricted range of temperature. Here I review the current status and correct an error in a recent book chapter.

Nature. 1975 Oct 16;257(5527):620-2. (PMID: 126384)
C R Trav Lab Carlsberg. 1961;32:185-214. (PMID: 14451942)
Phys Chem Chem Phys. 2012 Jan 7;14(1):318-26. (PMID: 22080213)
Biochemistry. 2014 Dec 9;53(48):7445-58. (PMID: 25407689)
J Org Chem. 2017 Mar 3;82(5):2307-2318. (PMID: 28102668)
J Phys Chem. 1971 May 13;75(10):1387-401. (PMID: 5554125)
Bioresour Technol. 2016 Dec;222:513-516. (PMID: 27720331)
J Chem Inf Comput Sci. 2001 Sep-Oct;41(5):1141-4. (PMID: 11604015)
J Biosci. 2002 Mar;27(2):121-6. (PMID: 11937682)
Protein Sci. 2001 Mar;10 (3):661-7. (PMID: 11344335)
Phys Chem Chem Phys. 2016 Jun 22;18(25):16690-9. (PMID: 27270406)
Biopolymers. 1970;9(10):1125-227. (PMID: 4918636)
Protein Sci. 2011 Sep;20(9):1607-18. (PMID: 21739503)
Biophys Chem. 2001 Nov 28;93(2-3):215-30. (PMID: 11804727)
J Phys Chem A. 2016 Oct 6;120(39):7598-7609. (PMID: 27615669)
J Phys Chem B. 2016 Oct 3;:null. (PMID: 27607917)
Dalton Trans. 2011 Aug 28;40(32):8059-71. (PMID: 21629958)

0 (Fish Proteins)
EC 3.6.1.- (Adenosine Triphosphatases)

Date Created: 20171213 Date Completed: 20180720 Latest Revision: 20190918

20221213

10.1007/s12038-017-9719-0

29229884