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. Author manuscript; available in PMC: 2018 Mar 1.
Published in final edited form as: Biochim Biophys Acta. 2016 Dec 6;1862(3):283–290. doi: 10.1016/j.bbalip.2016.12.001

Table 1.

Steady state kinetic analysis of LmBuk at 37°C.

Substrate kcat (min−1) KM (mM) kcat / KM (mM−1min−1)
Straight-chain
Propionate 155.6 ± 0 174.1 ± 68.9 0.89
Butyrate 50.2 ± 0.4 50.5 ± 5.8 0.99
Pentanoate 71.7 ± 2.2 13.1 ± 3.3 5.5
Hexanoate 1310.9 ± 474.9 1856 ± 676 0.7
Branched-chain
Iso butyrate 23.7 ± 0.4 7.6 ± 1.3 3.1
Isovalerate 25 ± 0.1 57.1 ± 9.6 0.44
2-methylbutyrate 15.9 ± 1.5 36.2 ± 5.2 0.44
2-ethyl butyrate 6.7 ± 1.7 16.5 ± 0.9 0.4
2-methyl pentanoate 18.8 ± 2.4 44.2 ± 8.5 0.4
3-methyl pentanoate 21.2 ± 0.4 27.3 ± 0.8 0.8

Initial velocities were measured at 37 °C in the presence of 10 mM ATP at pH 7.5. The kcat and KM were calculated from the least squares fit of the experimental data from the different substrates to the Michaelis-Menten equation. The values indicated are the mean of experiments performed at least in triplicate ± SEM.