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Table 2 Dalziel steady-state kinetic parameters of native and refolded G6PD.

From: An optimised system for refolding of human glucose 6-phosphate dehydrogenase

 

Native G6PD

Refolded G6PD

Specific activity (IU/mg)

180 ± 10

175 ± 12

Ï•o(s)

0.00366 ± 0.00023

0.00358 ± 0.00031

ϕNADP+(μMs)

0.0259 ± 0.0041

0.0249 ± 0.0037

ϕG6P(μMs)

0.191 ± 0.021

0.196 ± 0.026

ϕNADP+G6P(μM2s)

1.61 ± 0.22

1.55 ± 0.18

ϕNADP+G6P/ϕNADP+(μM)

57.98 ± 0.68

62.6 ± 3.4

ϕNADP+G6P/ϕG6P(μM)

7.77 ± 0.68

7.90 ± 0.37

kcat(s-1)

275 ± 18

279 ± 6.8

KmNADP+(μM)

7.07 ± 1.13

6.94 ± 0.34

KmG6P(μM)

52 ± 4

54.7 ± 3.2

kcat/KmNADP+(μM-1 s-1)

39.7 ± 7.5

40.3 ± 2.5

kcat/KmG6P(μM-1 s-1)

5.31 ± 0.69

5.1 ± 0.34

  1. The table shows the four constants of the reciprocal initial-rate equation [26] as estimated for wild-type G6PD and refolded enzyme. The corresponding of kcat values and the true Km values for both substrates are also listed. The parameters in each case were obtained from three independent experiments.
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BMC Biotechnology

ISSN: 1472-6750

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