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