enzyme efficient biocatalytic synthesis system is developed for the phosphorylation of D-tagatose 6-phosphate at its C1-position using the recombinant D-tagatose 6-phosphate kinase and the phosphoenolpyruvate/pyruvate kinase-system for ATP regeneration. This straightforward and scalable one-step biocatalytic synthesis of D-tagatose 1,6-diphosphate is successfully scaled up to the gram scale. Method evaluation and optimization, production analysis by NMR spectroscopy, overview
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high resolution structures of D-tagatose-6-phosphate kinase (LacC) in two crystal forms. The structures define LacC in apoform, in binary complexes with ADP or the cofactor analogue adenosine 5'-(beta,gamma-imino)triphosphate, and in a ternary complex with adenosine 5'-(beta,gamma-imino)triphosphate and D-tagatose-6-phosphate. LacC adopts a closed structure required for phosphoryl transfer only when both substrate and co-factor are bound
native and L124M, L125M double mutant crystallized by hanging drop vapor diffusion method in apoform, in binary complexes with ADP or the cofactor analogue AMP-PNP, and in a ternary complex with AMP-PNP and D-tagatose-6-phosphate, wild-type protein give crystals that diffracte only to low resolution, the SeMet double mutant protein produced much more ordered crystals