Researchers at the Technical University of Munich (TUM) have uncovered a novel mechanism affecting enzyme activity, revealing how the sequence of molecular binding can significantly impact their function. The findings, published in the journal “Nature Communications”, highlight a phenomenon known as substrate inhibition, where enzymes become temporarily less effective when overwhelmed by an excess of molecules.
The research team investigated an enzyme found in tobacco plants responsible for producing defense compounds. Their study demonstrated that when a phenol molecule initially binds to the enzyme, it results in a subsequent inhibition of its activity. Notably, beta-carotene was observed to mitigate this inhibitory effect by competing with the phenol for binding sites.
The TUM scientists emphasized that beta-carotene isn’t a universal solution for enzyme inhibition, cautioning against broad application. The research underscores the importance of the binding order of molecules to the enzyme’s overall performance.
Looking ahead, these findings have the potential for long-term applications in diverse fields. They could contribute to advancements in medicine, potentially impacting drug efficacy, or in industry, optimizing the efficiency of various industrial processes. The team believes further investigation into this mechanism could unlock new avenues for targeted interventions and improved performance in biological and industrial systems.