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. Author manuscript; available in PMC: 2018 May 17.
Published in final edited form as: FEBS Lett. 2017 Apr 17;591(9):1212–1224. doi: 10.1002/1873-3468.12630

Table 1.

Apparent kinetic constants for the reaction catalyzed by CysE in the absence and presence of CysK at fivefold molar excess over CysE. When acetyl-CoA was the varied substrate the concentration of L-Ser was 20 mM. When L-Ser was the varied substrate, the concentration of acetyl-CoA was 0.25 mM. The concentration of CysE for the calculation of kcat is based on the hexameric complex.

Varied substrate Kinetic constants −CysK +CysK
Acetyl-CoA KM (mM)  1.4 ± 0.4  0.8 ± 0.2
kcat (s−1) 306 ± 35 416 ± 38
kcat/KM (mM−1·s−1) 212 ± 83 501 ± 148
L-Ser KM (mM)  1.7 ± 0.7  1.1 ± 0.4
kcat (s−1) 228 ± 60 228 ± 34
kcat/KM (mM−1·s−1) 134 ± 90 207 ± 106
Ki,L-Ser (mM)  3.7 ± 1.4   16 ± 5