Table 1 Comparative kinetic parameters of recombinant LdG6PD wt and mutants, LmG6PD, TcG6PD, PfGluPho, and HsG6PD.

From: Crystal structure of Leishmania donovani glucose 6-phosphate dehydrogenase reveals a unique N-terminal domain

 

G6P

NADP+

 

Vmax (U · mg−1)

KM (µM)

kcat (s−1)

kcat/KM

(µM−1 · s−1)

Vmax (U · mg−1)

KM (µM)

kcat (s−1)

kcat/KM

(µM−1 · s−1)

LdG6PDDimer

200.0 ± 14.1

54.4 ± 2.8

222.5 ± 15.7

4.1 ± 0.2

204.7 ± 13.3

15.9 ± 1.1

227.7 ± 14.8

14.5 ± 1.6

LdG6PDTetramer

189.2 ± 7.7

75.4 ± 5.5

208.1 ± 5.1

2.8 ± 0.2

185.1 ± 12.9

14.2 ± 0.9

203.6 ± 13.6

14.9 ± 3.0

LdG6PDC138S

228.1 ± 12.5

63.3 ± 2.3

253.6 ± 13.9

4.0 ± 0.1

224.7 ± 13.8

14.6 ± 1.6

249.8 ± 15.3

17.3 ± 0.8

LdG6PD60–562

239.8 ± 10.6

65.4 ± 3.5

240.8 ± 10.6

3.7 ± 0.1

232.7 ± 18.7

14.3 ± 2.2

233.7 ± 18.8

17.0 ± 2.5

LmG6PD

187.0 ± 2.8

57.9 ± 4.6

208.1 ± 3.1

3.6 ± 0.3

187.7 ± 1.6

11.4 ± 1.5

208.8 ± 1.8

17.9 ± 3.5

TcG6PD29,39

99.4 ± 9.1

77 ± 20

62 ± 3

0.81

99.4 ± 9.1

16 ± 3

52 ± 2

3.3

PfGluPho24

5.9 ± 1.0

20.3 ± 5.6

10.7 ± 1.8

0.53

5.9 ± 0.6

6.1 ± 1.3

10.1 ± 0.9

1.66

HsG6PD

113.8 ± 6.7

70.1 ± 15.5

118.9 ± 7.0

1.7 ± 0.3

105.8 ± 7.2

22.9 ± 2.8

110.5 ± 7.6

5.0 ± 0.7

  1. Values are expressed as mean ± SD from at least three independent determinations with different enzyme batches; each including at least three measurements.
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