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. Author manuscript; available in PMC: 2012 Nov 1.
Published in final edited form as: Bioorg Med Chem. 2011 Aug 30;19(21):6447–6453. doi: 10.1016/j.bmc.2011.08.056

Table 3.

Kinetic parameters for KHO cleavage catalyzed by selected EC KDPG aldolase mutants.*

Mutant Mutations kcat
(s−1)		 KM
(mM)		 kcat/KM
(M−1s−1)
wt-ECA none 2 ± 0.6 150 ± 50 14 ± 4
EC 9 V17L/E51K/P94L/G124M/L173M -- -- > 0.1
EC 10 V17L/V23I/E51K/P94L/F134I/L173M/D190E -- -- > 0.2
EC 11 V17L/A53T/P94L/V118L/A137T/L173M 0.01 ± 0.005 1.5 ± 0.4 10 ± 3
*

Initial velocity for pyruvate formation was measured using a lactate dehydrogenase coupled assay at 25 °C. Steady state kinetic parameters were determined by fitting of the Michaelis-Menten equation to the initial velocity as a function of the substrate concentration.