It’s a knock-in

New research from the School of Chemistry has advanced our understanding of how enzymes (proteins) increase the rate of chemical reactions.

Enzymes are fundamental to life. They are proteins that catalyse chemical reactions, for example in metabolic processes to release of energy from foods and in cell growth and repair. Enzymes often increase reaction rates several trillion fold; they find uses in industries such as food, cosmetics, detergents, pharmaceuticals and chemical manufacturing.

A team led by Professor Allemann, Distinguished Research Professor and Head of Cardiff's School of Chemistry, and their colleagues at the University of València and Jaume I University in Castelló had previously demonstrated that enzyme motions do not directly help increase the rate of the catalysed reaction. Their new research has now shown that motions can in fact be detrimental to an enzyme's function. The team used a combination of experimental and computational methods to study a variant enzyme with impaired activity and greatly reduced slow internal motions (millisecond timescale). They now show that increased fast motions (femtosecond time scale) are responsible for the loss of activity. Therefore, although the enzyme is a 'dynamic knockout' on a millisecond timescale, it is a 'dynamic knock-in' at timescales relevant to chemical reactions.

The work, recently published in the Journal of the American Chemical Society, greatly advances our understanding of enzyme catalysis. A thorough understanding of how enzymes achieve their phenomenal rate enhancements – typically much more effectively and under more environmentally friendly conditions than man made catalysts – is an important goal in biotechnology, with great importance to fields like biocatalysis, bioenergy, drug design and the emerging field of synthetic biology.