Rapid bursts and slow declines: on the possible evolutionary trajectories of enzymes.
The evolution of enzymes is often viewed as following a smooth and steady trajectory, from barely functional primordial catalysts to the highly active and specific enzymes that we observe today. In this review, we summarize experimental data that suggest a different reality. Modern examples, such as the emergence of enzymes that hydrolyse human-made pesticides, demonstrate that evolution can be extraordinarily rapid. Experiments to infer and resurrect ancient sequences suggest that some of the first organisms present on the Earth are likely to have possessed highly active enzymes. Reconciling these observations, we argue that rapid bursts of strong selection for increased catalytic efficiency are interspersed with much longer periods in which the catalytic power of an enzyme erodes, through neutral drift and selection for other properties such as cellular energy efficiency or regulation. Thus, many enzymes may have already passed their catalytic peaks.
Department of Biochemistry, University of Otago, Dunedin, New Zealand.
Matilda S
MS
Newton
School of Biology, University of Waikato, Hamilton, New Zealand.
Vickery L
VL
Arcus
Department of Biochemistry, University of Otago, Dunedin, New Zealand wayne.patrick@otago.ac.nz.
Wayne M
WM
Patrick
D001419:Bacteria / Q000201:enzymology / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D004798:Enzymes / Q000235:genetics* / Q000378:metabolism; D019143:Evolution, Molecular; D006801:Humans; D008957:Models, Genetic; D010575:Pesticides / Q000494:pharmacology
D001426:Bacterial Proteins; D004798:Enzymes; D010575:Pesticides
activity threshold; adaptive evolution; ancestral sequence reconstruction; catalytic efficiency