Enzymes are the molecular machines driving life’s biochemistry – but their performance depends heavily on the molecules surrounding them. A new study by researchers at Ruhr University Bochum (RUB) and the Research Center Chemical Sciences and Sustainability reveals that chemical interactions, not just molecular crowding, are key to keeping enzymes functional when temperatures rise.
The scientists investigated phosphofructokinase-1 (PFKP), a critical enzyme in glucose metabolism. While crowded environments typically hinder enzyme activity at lower temperatures, the researchers found that sugar-based molecules (like glucose and dextran) helped PFKP retain activity at higher temperatures – regardless of their size. Molecular simulations suggested these molecules subtly influence enzyme flexibility and substrate positioning through weak, reversible interactions near the active site.
The findings, published in the international edition of ‘Angewandte Chemie’, hint that cells may fine-tune metabolic resilience by adjusting their local chemical landscapes.