Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the P<sub><i>i</i></sub>. Scott Mazurkewich Stephen Y. K. Seah 10.1371/journal.pone.0164556.t003 https://plos.figshare.com/articles/dataset/Steady_state_kinetic_parameters_of_HMG_lyase_activity_of_variants_of_the_HMG_CHA_aldolase_in_the_presence_or_absence_of_the_P_sub_i_i_i_sub_/4034538 <p>Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the P<sub><i>i</i></sub>.</p> 2016-10-14 17:34:35 class II Phosphate Activation enzyme P i activation CHA K M Putative P i binding residues acid half reaction P i saturation kinetics HMG site-directed mutagenesis presence Pseudomonas putida F 1 acid water site 4- hydroxy -4-methyl 1 mM P i divalent metal rate enhancement class II aldolase 4- Hydroxy -4-Methyl Aldolase aldolase pyruvate methyl proton exchange rate P i binding site phosphate activation Docking studies