Temperature, Dynamics, and Enzyme-Catalyzed Reaction Rates

Vickery L Arcus, Adrian J Mulholland

Research output: Contribution to journalArticle (Academic Journal)peer-review

62 Citations (Scopus)


We review the adaptations of enzyme activity to different temperatures. Psychrophilic (cold-adapted) enzymes show significantly different activation parameters (lower activation enthalpies and entropies) from their mesophilic counterparts. Furthermore, there is increasing evidence that the temperature dependence of many enzyme-catalyzed reactions is more complex than is widely believed. Many enzymes show curvature in plots of activity versus temperature that is not accounted for by denaturation or unfolding. This is explained by macromolecular rate theory: A negative activation heat capacity for the rate-limiting chemical step leads directly to predictions of temperature optima; both entropy and enthalpy are temperature dependent. Fluctuations in the transition state ensemble are reduced compared to the ground state. We show how investigations combining experiment with molecular simulation are revealing fundamental details of enzyme thermoadaptation that are relevant for understanding aspects of enzyme evolution. Simulations can calculate relevant thermodynamic properties (such as activation enthalpies, entropies, and heat capacities) and reveal the molecular mechanisms underlying experimentally observed behavior.

Original languageEnglish
Pages (from-to)163-180
Number of pages18
JournalAnnual review of biophysics
Early online date4 Feb 2020
Publication statusPublished - 6 May 2020

Bibliographical note

The acceptance date for this record is provisional and based upon the month of publication for the article.


Dive into the research topics of 'Temperature, Dynamics, and Enzyme-Catalyzed Reaction Rates'. Together they form a unique fingerprint.

Cite this