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Comparison of the catalytic efficiency of Asp1 kinase and pyrophosphatase activities
| Species | Construct | Reaction | Km, µM | Vmax, nmol/min/mg | kcat, s−1 | kcat/Km, 103 M−1⋅s−1 |
| S. pombe | Asp1-FL | Kinase | 4.6 | 5.8 | 0.010 | 2.2 |
| S. pombe | Asp1-FL | Pyrophosphatase | 0.47 | 9.3 | 0.016 | 33 |
Kinetic constants were determined by fitting enzyme activity determinations of at least three independent measurements by nonlinear regression to the following equation: Y = Vmax*X/(KM + X). Assays were performed at pH 7.0.
