Bengt Mannervik

Department of Biochemistry and Biophysics, Stockholm University

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INPEC node since 2008​

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Mannervik’s most influential contributions concern glutathione reductase and the glutathione transferase (GST) superfamily, enzymes that play a central role in protecting cells from toxic substances. His work elucidated the structural diversity, catalytic mechanisms, and physiological functions of these enzymes, demonstrating how they detoxify reactive compounds produced both within organisms and in the external environment. By establishing GSTs as a model system, he helped define fundamental principles of enzyme specificity, efficiency, and regulation. 

 

Beyond defining detoxication pathways, Mannervik made significant contributions to molecular toxicology, demonstrating that enzymatic processes govern the metabolism of drugs, carcinogens, and environmental toxins. His research revealed that variations in these enzyme systems can influence individual susceptibility to disease and response to therapy, thereby linking biochemical mechanisms to medical outcomes. In general enzymology Mannervik contributed advances in discrimination between rival kinetic models based on nonlinear regression analysis. 

 

A further dimension of his work addresses the molecular evolution and engineering of enzymes. By investigating how catalytic functions emerge and diversify, he demonstrated that enzymes possess remarkable adaptability. His studies of glutathione transferases provided important insights into protein evolution and enabled the design of enzymes with novel or enhanced functions for translational applications in medicine and biotechnology. ​

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Keywords: glutathione enzymology, molecular design and evolution