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Table 3 Apparent kinetic constants of recombinant and wild-type Glomerella cingulata GDH for either D-glucose or D-xylose as substrate, with the concentration of the electron acceptor ferrocenium ion held constant at 20 μM.

From: Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris

Substrate and pH enzyme Km
(mM)
kcat
(s-1)
kcat/Km
(M-1 s-1)
Glucose, pH = 5.5 wt 10.2 ± 0.2 180 ± 3 17.6 × 103
  rec 10.1 ± 0.4 179 ± 4 17.7 × 103
Glucose, pH = 7.5 wt 19.0 ± 0.3 380 ± 6 20.0 × 103
  rec 17.1 ± 0.7 418 ± 4 24.5 × 103
Xylose, pH = 5.5 wt 21 ± 0.6 40 ± 1.5 1.90 × 103
  rec 26 ± 2.7 53 ± 1.9 2 × 103
Xylose, pH = 7.5 wt 24 ± 1.5 60 ± 2 2.5 × 103
  rec 23 ± 0.7 61 ± 1 2.7 × 103
  1. Kinetic data were determined at 30°C, the data for wild-type Gc GDH are from [10].