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Probing The Allosteric Activation Of Pyruvate Carboxylase Using 2′,3′-O-(2,4,6-Trinitrophenyl) Adenosine 5′-Triphosphate As A Fluorescent Mimic Of The Allosteric Activator Acetyl Coa, Abdussalam Adina-Zada, Rasmani Hazra, Chutima Sereerukb, Sarawut Jitrapakdee, Tonya N. Zeczycki, Martin St. Maurice, W Wallace Cleland, John C. Wallace, Paul V. Attwood
Probing The Allosteric Activation Of Pyruvate Carboxylase Using 2′,3′-O-(2,4,6-Trinitrophenyl) Adenosine 5′-Triphosphate As A Fluorescent Mimic Of The Allosteric Activator Acetyl Coa, Abdussalam Adina-Zada, Rasmani Hazra, Chutima Sereerukb, Sarawut Jitrapakdee, Tonya N. Zeczycki, Martin St. Maurice, W Wallace Cleland, John C. Wallace, Paul V. Attwood
Biological Sciences Faculty Research and Publications
2′,3′-O-(2,4,6-Trinitrophenyl) adenosine 5′-triphosphate (TNP-ATP) is a fluorescent analogue of ATP. MgTNP-ATP was found to be an allosteric activator of pyruvate carboxylase that exhibits competition with acetyl CoA in activating the enzyme. There is no evidence that MgTNP-ATP binds to the MgATP substrate binding site of the enzyme. At concentrations above saturating, MgATP activates bicarbonate-dependent ATP cleavage, but inhibits the overall reaction. The fluorescence of MgTNP-ATP increases by about 2.5-fold upon binding to the enzyme and decreases on addition of saturating acetyl CoA. However, not all the MgTNP-ATP is displaced by acetyl CoA, or with a combination of saturating concentrations of …