Table 2 Longitudinal relaxation times of 13C sites* in [13C6,D8]2DG and [13C6,D7]glucose during phosphorylation reactions.

From: [13C6,D8]2-deoxyglucose phosphorylation by hexokinase shows selectivity for the β-anomer

Compound & Enzyme

Apparent T1 of C1β (s)

Apparent T1 of C1α (s)

T1 of C6P (s)

T1 of C6 (s)

Apparent T1 of C2β (s)

Apparent T1 of C2α (s)

[13C6,D8]2DG & yHKa, #

8.8 ± 0.3

12.8 ± 1.1

7.2 ± 0.6

9.7 ± 0.2

5.9 ± 0.3

8.4 ± 0.8

[13C6,D8]2DG & bGKb **

22.3 ± 2.1

22.0 ± 1.7

Not detected

12.6 ± 3.3

15.3 ± 0.6

15.1 ± 0.8

[13C6,D7]glucose & yHKc

10.3 ± 0.5

10.0 ± 0.4

6.4 ± 0.3

7.9 ± 0.1

Not resolved

Not resolved

[13C6,D7]glucose & bGKc **

14.0 ± 0.8

14.8 ± 1.4

9.8 ± 1.6

13.0 ± 1.9

Not resolved

Not resolved

  1. Values are presented as mean ± standard deviation.
  2. #Differences in the apparent T1 between the β and α anomers for the C1 and C2 positions were 31% (p = 0.00004) and 29% (p = 0.0002), respectively. p-values were calculated using a paired t-test.
  3. *Only sites that could be spectrally resolved were analyzed. The apparent T1 calculation (Methods) for the C1 and C2 sites was done without taking into consideration the reaction kinetics as the substrate and product signals were not resolved for this site. For the C6 position, a full kinetic analysis was performed and the reaction kinetic rate constant are provided in Supplementary Information S2.
  4. **Experiments with bGK were performed at 40 °C. Experiments with yHK were performed at room temperature (ca. 21 °C). (a) n = 5; (b) n = 2 (no reaction); (c) n = 4.
  5. C6P, C6 position of the phosphorylated product; C6, C6 position of the substrate.
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