. Author manuscript; available in PMC: 2017 Sep 1.

Published in final edited form as: Biochim Biophys Acta. 2016 Jun 15;1861(9 Pt A):1102–1110. doi: 10.1016/j.bbalip.2016.06.003

Table 1.

Steady state kinetic analysis of Ptb from L. monocytogenes

Substrate	k_cat (sec⁻¹)	K_M (µM)	k_cat/K_M (µM⁻¹sec⁻¹)
Straight-chain
Acetyl CoA	302.4 ±103.9	992.1 ± 471.9	0.3
Propionyl CoA	518.8 ± 25.8	190.6 ± 20.9	2.72
Butyryl CoA	673.9 ± 25.2	79.9 ± 8.8	8.43
Pentanoyl CoA	676.1 ± 19	160.8 ± 10.5	4.2
Hexanoyl CoA	47 ± 2.6	31.5 ± 8.4	1.7
Branched-chain
Iso butyryl CoA	1263.4 ± 31.7	57.9 ± 4.8	21.4
Isovaleryl CoA	1043.4 ± 12.2	53.2 ± 2.1	19.6
2-methylbutyryl CoA	849.1 ±18	48.1 ± 3.4	17.7
2-ethyl butyryl CoA	100.9 ± 11	43.8 ± 20.3	2.3

Initial velocities were measured at 25 °C in the presence of 100 mM phosphate at pH 7.5. The k_cat and K_M 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.