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- W1546249675 abstract "We have developed a highly sensitive assay of MEK-mediated ATP hydrolysis by coupling the formation of ADP to NADH oxidation through the enzymes pyruvate kinase and lactate dehydrogenase. Robust ATP hydrolysis is catalyzed by phosphorylated MEK in the absence of the protein substrate ERK. This ERK-uncoupled ATPase activity is dependent on the phosphorylation status of MEK and is abrogated by the selective MEK kinase inhibitor U0126. ADP production is concomitant with RAF-mediated phosphorylation of MEK. After initiation with catalytic amounts of an activated RAF enzyme and non-phosphorylated MEK, the reaction's progress curves are composed of an acceleration phase, associated mainly with RAF activity, and a terminal steady-state phase, associated with MEK activity. Selective inhibitors of RAF activity diminish the acceleration phase of the progress curve without direct affect on the steady state phase. This activity assay may thus be used to evaluate inhibitors of both RAF and MEK enzymatic activity." @default.
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- W1546249675 date "2007-04-01" @default.
- W1546249675 modified "2023-10-17" @default.
- W1546249675 title "An Intrinsic ATPase Activity of Phospho‐MEK‐1 Uncoupled from Downstream ERK Phosphorylation" @default.
- W1546249675 doi "https://doi.org/10.1096/fasebj.21.5.a640-d" @default.
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