Atomic structure of a bent sugar molecule in the human enzyme transketolase just before it splits. The blue star indicates a carbon atom of the sugar that has been distorted out of the expected position within the grey plane by over 20 degrees.
Göttingen scientists unravel fundamental mechanisms of biochemical reactions (pug) Enzymes are the molecular catalysts of life performing vital metabolic functions in every cell. To date, it has been speculated that enzymes literally bend and break their substrates during biochemical reactions. For the first time, scientists at the Göttingen Center for Molecular Biosciences (GZMB) succeeded in experimentally confirming this hypothesis with certainty. The results of this study were published in the prestigious. Led by Professor Kai Tittmann and Professor Ralf Ficner, the Göttingen scientists started off by growing highly ordered protein crystals of the human enzyme transketolase, which plays a pivotal role in human cellular sugar metabolism. They then added natural sugar substrates to these protein crystals. The structures of these enzyme crystals were analysed at particle accelerators located in Berlin, Germany and Grenoble, France.
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