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Fructose 1,6-bisphosphatase and gluconeogenesis control in an anoxia-tolerant turtle, Trachemys scripta elegans
  • Aakriti Gupta,
  • Anchal Varma,
  • Kenneth Storey
Aakriti Gupta
Carleton University Institute of Biochemistry
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Anchal Varma
Carleton University Institute of Biochemistry
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Kenneth Storey
Carleton University Institute of Biochemistry

Corresponding Author:[email protected]

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Abstract

The red eared slider ( Trachemys scripta elegans) undergoes numerous changes to its physiological and metabolic processes to survive without oxygen. During anoxic conditions, its metabolic rate drops drastically to minimise energy requirements. The alterations in central metabolic pathways are often accomplished by the regulation of key enzymes. The regulation of one such enzyme, fructose-1,6-bisphosphatase (FBPase; EC 3.1.3.11), was characterized in the present study during anoxia in liver. FBPase is a crucial enzyme of gluconeogenesis. FBPase was purified from liver tissue in both control and anoxic conditions and subsequently assayed to determine the kinetic parameters of the enzyme. Studies revealed the relative degree of posttranslational modifications in FBPase from control and anoxic turtles. Further, this study demonstrated a significant decrease in the maximal activity in anoxic FBPase and decreased sensitivity to its substrate fructose-1,6-bisphosphate (FBP) when compared to the control. Immunoblotting demonstrated increased threonine phosphorylation (~1.4 fold) in the anoxic FBPase. Taken together these results suggest that phosphorylation of liver FBPase is an important step in suppressing FBPase activity ultimately leading to inhibition of gluconeogenesis in the liver of the red eared slider during anaerobic conditions.