Table 1 Kinetic parameters for the activity of wild-type mIDH2 (WT) and the K256Q and K413Q mutants.

From: Studies on the regulatory mechanism of isocitrate dehydrogenase 2 using acetylation mimics

Enzyme

K m (μM)

V max (μM s−1)

k cat (s−1)

k cat /K m (s−1 μM−1)

(Kinetic parameters for isocitrate)

   WT

54.4 ± 5.6a

0.028 ± 0.001

5.60 ± 0.14

0.111 ± 0.011

   K256Q

30.4 ± 2.3

0.013 ± 0.0002

2.66 ± 0.04

0.088 ± 0.008

   K413Q

55.5 ± 7.1

0.023 ± 0.001

4.61 ± 0.15

0.083 ± 0.008

(Kinetic parameters for NADP+)

   WT

33.7 ± 2.4

0.031 ± 0.0006

6.36 ± 0.14

0.186 ± 0.011

   K256Q

14.8 ± 1.3

0.015 ± 0.0003

3.13 ± 0.13

0.205 ± 0.022

   K413Q

112.2 ± 13.2

0.033 ± 0.001

7.69 ± 0.49

0.059 ± 0.001

  1. aValues are the means of four technically independent replicates and are displayed as the means ± SD.
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