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. 2017 Sep 29;83(20):e01251-17. doi: 10.1128/AEM.01251-17

TABLE 5.

Kinetic parameters toward MFAd

Enzyme kcat (s−1) Km (mM) kcat/Km (s−1 mM−1)
W160P mutanta >10 4.2 × 10−4 ± 0.3 × 10−4
W160S mutanta >10 1.4 × 10−3 ± 0.5 × 10−3
W160A mutant 8.4 × 10−3 ± 1.1 × 10−3 8.3 ± 0.2 1.0 × 10−3 ± 0.4 × 10−3
Y39G/W160P mutant 3.2 × 10−2 ± 0.5 × 10−2 8.0 ± 2.0 4.0 × 10−3 ± 0.2 × 10−3
Y39P/W160S mutant 3.1 × 10−2 ± 0.3 × 10−2 6.6 ± 1.2 4.8 × 10−3 ± 0.1 × 10−3
NcFAE1b 5.2 0.25 21
PfFAEBc 16 0.047 340
a

The Km and kcat values could not be confidently determined due to the solubility limits of the substrate (10 mM).

b

Data from Crepin et al. (23).

c

Data from Kroon et al. (22).

d

Activities were measured in 95 mM potassium phosphate buffer (pH 7.0) at 37°C.