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Adjusting to High Temperatures: Researchers Discover Multifunctional Enzyme Active in Metabolism

Gluconeogenesis is the ability to re-synthesize sugar out of simpler chemical building blocks. It is a central pathway of the metabolism in humans as well as simple bacteria. Researchers have been unable to scientifically analyse this conclusively until now.

Together with the research groups led by Prof. Dr. Oliver Einsle at the Institute of Organic Chemistry and Biochemistry and Prof. Dr. Georg Fuchs from the Institute of Biology II, research groups at the Centre for Biological Signalling Studies (BIOSS), the Spemann Graduate School of Biology and Medicine (SGBM) and the Freiburg Institute of Advanced Studies (FRIAS) have described a fundamentally new type of multifunctional enzyme in this metabolic pathway.
Their new findings have now been published online in the current issue of the journal Nature.

The researchers discovered that the entire field of archaea organisms, which are so-called ancient bacteria, lacks aldolase, which is a key enzyme in gluconeogenesis. In 2010, Dr. Rafael Say and Dr. Georg Fuchs discovered that the enzyme fructose-1,6-bisphosphate can also perform the functions of aldolase, even though the enzyme’s amino acids involved in the aldolase reaction are far removed from the binding site of the substrate.

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