TABLE 1.
Comparison of wild-type and mutant FlK
Enzyme reactions were carried out using FAcCoA as the substrate. Errors quoted represent the S.E. of curve fitting (Lineweaver-Burk plot). Each data point is the average of four (WtFlK), three (T42SFlK), or two E50AFlK measurements.
Protein | Soluble protein | kcata | Km | kcat/Kmb | FAcCoA concentration above which substrate inhibition was observed |
---|---|---|---|---|---|
mg/liter | s−1 | μm | mm−1s−1 | μm | |
WtFlK | ∼10–12 | 0.044 ± 0.001 | 30 ± 1.3 | 1.47 ± 0.10 | |
T42SFlK | ∼10–12 | 0.409 ± 0.159 | 15 ± 1.2 | 27.3 ± 12.8 | 12 |
T42AFlK | ∼2 | ||||
E50AFlK | ∼2 | 0.111 ± 0.041 | 206 ± 67 | 0.54 ± 0.37 | 19 |
a The units are number of CoA released/s/enzyme molecule.
b The error values given for kcat/Km are calculated from the sum of the relative errors on values in the numerator and denominator.