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. 2021 May 7;60(24):13302–13309. doi: 10.1002/anie.202102690

Figure 5.

Figure 5

Real‐time enzyme kinetics by 19F NMR using F‐glycans. A) 19F NMR of F‐Lac incubated with β‐galactosidase. 19F NMR real‐time tracking of product formation (black arrows) upon incubation of F‐Lac with β‐galactosidase (right). Kinetic data were derived plotting the product formation rate as a function of the substrate concentration. The best fit of the experimental data provides a K M value of 86.5±10.5 μm according to the Henry‐Michaelis–Menten equation (left). B) 19F NMR of F‐Lac incubated with Pmα23ST in presence of CMP‐Neu5Ac. The formation of F‐sLac (black arrows) can be followed by 19F NMR in real‐time. Product formation was confirmed by HPLC (Figure S9).