Journal
FEBS LETTERS
Volume 589, Issue 13, Pages 1444-1449Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2015.04.042
Keywords
ADP-glucose pyrophosphorylase; Substrate binding properties; Heterotetramer; Homotetramer; Isothermal titration calorimetry; Starch synthesis
Funding
- Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the United States Department of Energy [DE-FG02-12ER20216]
- Agricultural Research Center, College of Agricultural, Human, and Natural Resource Sciences, Washington State University [0590]
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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 ((SLWT)-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 ATP gamma S suggesting that interaction of glucose-1-phosphate is dependent on hydrolysis of ATP and supports the Theorell-Chance bi bi reaction mechanism. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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