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. 2010 Apr 29;285(29):22495–22504. doi: 10.1074/jbc.M110.107177

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 s1 μm mm1s1 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.