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Enzymes can adapt to cold by wiggling regions far from their active site

Mutations introduced far from the active site of an enzyme can cause local unfolding that increases enzyme activity. This finding suggests how organisms that live in the cold can speed up biochemical reactions.
  1. Ashok A. Deniz

    1. Ashok A. Deniz is in the Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

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The biochemical sciences have tended to focus on processes that take place at ‘physiological’ temperatures of around 37 °C. But much of Earth’s surface is covered with ocean, ice or snow, and is replete with organisms that function at much lower temperatures. Life in these environments requires suitable biological adaptations, for example in the enzymes that maintain the chemical environment of the cell. In a paper in Nature, Saavedra et al.1 shed light on a biophysical mechanism for such low-temperature adaptation that operates at the molecular level. Their results show strikingly that protein modifications distant from an enzyme’s active site can modulate localized unfolding of the enzyme — effectively, wiggling of parts of the enzyme’s structure — that can control several facets of enzyme-reaction mechanisms.

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Nature 558, 195-196 (2018)

doi: https://doi.org/10.1038/d41586-018-05302-x

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