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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
ϕo(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+G6PNADP+(μM) 57.98 ± 0.68 62.6 ± 3.4
ϕNADP+G6PG6P(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.