Figure 3
From: [13C6,D8]2-deoxyglucose phosphorylation by hexokinase shows selectivity for the β-anomer
Phosphorylation reactions of [13C6, D7]glucose by yHK and bGK. (A) A 13C spectrum showing all of the signals of hyperpolarized [13C6,D7]glucose and [13C6,D7]G6P during the reaction with yHK. The chemical shift was referenced to C1β at 97.4 ppm77. (B) Consecutive 13C spectra of a typical experiment with yHK. The chemical shift regions of the C1 and C6 signals of both [13C6,D7]glucose and [13C6,D7]G6P are presented. (C) The time course of the integrated signal intensities for the experiment shown in B. (D) Consecutive 13C spectra of a typical experiment with bGK. The chemical shift regions of the C1 and C6 signals of both [13C6,D7]glucose and [13C6,D7]G6P are presented. (E) The time course of the integrated signal intensities for the experiment shown in D. (F) Consecutive 13C spectra of a typical experiment without an enzyme. The chemical shift regions of the C1 and C6 signals of both [13C6,D7]glucose and [13C6,D7]G6P are presented. (G) The time course of the integrated signal intensities for the experiment shown in F. The spectra were collected over 50 s after the addition of hyperpolarized [13C6,D7]glucose, with a repetition time of 1 s and a 10° flip angle. yHK – yeast hexokinase, b GK - bacterial glucokinase, w/o - without, Intensity - integrated signal intensity, a.u. - arbitrary units.
