Functional characterization of transketolase-like proteins and related model systems with respect to thiamin diphosphate mediated chemistry

TL;DRAbstract

Transketolases (TKTs, E.C 2.2.1.1) are ubiquitous distributed enzymes among all three domains of life. TKTs require thiamin diphosphate (ThDP) and bivalent cations as catalytic cofactors. They fulfill their catalytic function within several metabolic pathways, of which the calvin-cycle of photosynthetic plants and the pentose phosphate pathway (PPP) are the most important ones. The PPP is a cell’s main source of the reductive equivalent nicotine adenine dinucleotid phosphate (NADPH) and ribose 5-phosphate (R5P), the precursor for nucleotide-synthesis. By adjusting the balance of the metabolic flux within the PPP, a cell can adapt towards changing metabolic demands. This metabolic adaption is of particular interest in terms of cancerogenesis, since it has been shown, that cancerous cells seem to modify the generation of NADPH and R5P to force cell dividing capacity. In this regard TKT’s central role in the PPP is of great interest since inhibition of TKT was shown to have growth-inhibit

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