Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry
| Autor: | Bilal Cakir, Kaan Koper, ChulHee Kang, Abigail R. Green, Aytug Tuncel, Thomas W. Okita, Seon-Kap Hwang |
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| Jazyk: | angličtina |
| Předmět: |
Models
Molecular Blotting Western Biophysics Glucose-1-Phosphate Adenylyltransferase Calorimetry Substrate binding properties Biochemistry Binding Competitive Substrate Specificity Adenosine Triphosphate ADP-glucose pyrophosphorylase Structural Biology ATP hydrolysis Genetics Binding site Molecular Biology Heterotetramer Plant Proteins Solanum tuberosum chemistry.chemical_classification Binding Sites Molecular Structure Wild type Glucosephosphates Substrate (chemistry) Isothermal titration calorimetry Cell Biology Protein Structure Tertiary Kinetics Plant Tubers Protein Subunits Enzyme chemistry Thermodynamics Starch synthesis Protein Multimerization Homotetramer Protein Binding |
| Zdroj: | FEBS Letters. (13):1444-1449 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2015.04.042 |
| Popis: | 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 (SWTLWT) 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. |
| Databáze: | OpenAIRE |
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