Table 3.xls (9.5 kB)
Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi.
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posted on 2016-10-14, 17:34 authored by Scott Mazurkewich, Stephen Y. K. SeahSteady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi.
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class IIPhosphate ActivationenzymeP i activationCHAK MPutative P i binding residuesacid half reactionP isaturation kineticsHMGsite-directed mutagenesispresencePseudomonas putida F 1acid water site4- hydroxy -4-methyl1 mM P idivalent metalrate enhancementclass II aldolase4- Hydroxy -4-Methyl Aldolasealdolase pyruvate methyl proton exchange rateP i binding sitephosphate activationDocking studies
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