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Issue 46, 2015
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Protein motions and dynamic effects in enzyme catalysis

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Abstract

The role of protein motions in promoting the chemical step of enzyme catalysed reactions remains a subject of considerable debate. Here, a unified view of the role of protein dynamics in dihydrofolate reductase catalysis is described. Recently the role of such motions has been investigated by characterising the biophysical properties of isotopically substituted enzymes through a combination of experimental and computational analyses. Together with previous work, these results suggest that dynamic coupling to the chemical coordinate is detrimental to catalysis and may have been selected against during DHFR evolution. The full catalytic power of Nature's catalysts appears to depend on finely tuning protein motions in each step of the catalytic cycle.

Graphical abstract: Protein motions and dynamic effects in enzyme catalysis

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Article information


Submitted
07 Feb 2015
Accepted
30 Mar 2015
First published
09 Apr 2015

This article is Open Access

Phys. Chem. Chem. Phys., 2015,17, 30817-30827
Article type
Paper
Author version available

Protein motions and dynamic effects in enzyme catalysis

L. Y. P. Luk, E. J. Loveridge and R. K. Allemann, Phys. Chem. Chem. Phys., 2015, 17, 30817
DOI: 10.1039/C5CP00794A

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