LAUSR

Experiments and biomolecular simulations are revealing new and unexpected details of how enzymes are adapted to specific temperatures. These findings are elucidating enzyme evolutionary trajectories and offer great promise for design and engineering of natural and artificial enzymes. They also have implications for understanding responses of larger scale biological temperature dependence, relevant for understanding the effects of climate change on ecosystems. We review recent work on the temperature dependence of enzyme-catalysed reaction rates and the implications for enzyme evolution. Evidence from kinetic isotope effects, temperature dependent reaction rates, molecular dynamics simulations and thermodynamics provides new insights into enzyme thermoadaptation and evolution.