May 9, 2015

Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry

FEBS Letters
Bilal CakirChulHee Kang

Abstract

Substrate binding properties of the large (LS) and small (SS) subunits of potato tuber ADP-glucose pyrophosphorylase were investigated by using isothermal titration calorimetry. Our results clearly show that the wild type heterotetramer (S(WT)L(WT)) possesses two distinct types of ATP binding sites, whereas the homotetrameric LS and SS variant forms only exhibited properties of one of the two binding sites. The wild type enzyme also exhibited significantly increased affinity to this substrate compared to the homotetrameric enzyme forms. No stable binding was evident for the second substrate, glucose-1-phosphate, in the presence or absence of ATPγS suggesting that interaction of glucose-1-phosphate is dependent on hydrolysis of ATP and supports the Theorell-Chance bi bi reaction mechanism.

Mentioned in this Paper

ATP Binding
Thermodynamics
glucose-1-phosphate
Glycerin
Enzymes, antithrombotic
Hereditary Orotic Aciduria, Type 1
Amino Acids, I.V. solution additive
Analog
Tertiary Protein Structure
Macromolecular Alteration

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