Table 1 Kinetic constants of AceK and mutants with respect to phosphatase activities.

From: Characterization of metal binding of bifunctional kinase/phosphatase AceK and implication in activity modulation

Protein

Km (μM)

Kcat (s−1)

Kcat/Km (μM−1·s−1)

Ratio of Kcat/Km (WT/mutant)

WT

0.376 ± 0.054

122.6

326.1

1

D475A

1.946 ± 0.242

26.50

13.62

23.94

D477A

16.10 ± 2.650

21.88

1.359

240

D477K

12.17 ± 1.102

22.39

1.840

177.2

  1. The assays were performed in the 20 mM Hepes buffer pH 7.0 containing 2.0 mM Mn2+ and 2.0 mM ADP at 37 °C. The Kcat, Km and Kcat/Km values were fitted to the equation 2 using GraphPadPrism5 software. The data were repeated at least three times.
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