Temperature, Dynamics, and Enzyme-Catalyzed Reaction Rates.
Annu Rev Biophys
; 49: 163-180, 2020 05 06.
Article
in En
| MEDLINE
| ID: mdl-32040931
ABSTRACT
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Temperature
/
Enzymes
/
Biocatalysis
Type of study:
Prognostic_studies
Language:
En
Journal:
Annu Rev Biophys
Journal subject:
BIOFISICA
Year:
2020
Document type:
Article