A phosphoglycerate to inorganic phosphate ratio is the major factor in controlling starch levels in chloroplasts via ADP-glucose pyrophosphorylase regulation. Kleczkowski, L. A FEBS Letters, 448(1):153–156, 1999. _eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2899%2900346-4![A phosphoglycerate to inorganic phosphate ratio is the major factor in controlling starch levels in chloroplasts via ADP-glucose pyrophosphorylase regulation [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Purified barley leaf ADP-glucose pyrophosphorylase, a key enzyme of the starch synthesis in the chloroplast stroma, was analysed with respect to its possible regulation by factors defining the metabolic/effector status of the chloroplast during light and dark conditions. The enzyme required 3-phosphoglyceric acid for the maximal activity and was inhibited by inorganic phosphate. The optimal pH for the enzyme was at circa 7.0, regardless of the presence or absence of 3-phosphoglyceric acid, whereas the maximal activation by 3-phosphoglyceric acid was observed at pH 8.5 and higher. Changes in the concentration of Mg2+ and dithiothreitol had little or no effect on the enzymatic activity of AGPase. It has been directly demonstrated for the first time that a 3-phosphoglyceric acid/inorganic phosphate ratio, a crucial regulatory parameter, could be directly related to a defined activation state of the enzyme, allowing the prediction of a relative AGPase activity under given conditions. The predicted changes in the enzyme activity were directly correlated with earlier reported responses of starch levels to the 3-phosphoglyceric acid/inorganic phosphate ratio in chloroplasts. Consequences of this for the starch biosynthesis are discussed.
@article{kleczkowski_phosphoglycerate_1999,
title = {A phosphoglycerate to inorganic phosphate ratio is the major factor in controlling starch levels in chloroplasts via {ADP}-glucose pyrophosphorylase regulation},
volume = {448},
copyright = {FEBS Letters 448 (1999) 1873-3468 © 2015 Federation of European Biochemical Societies},
issn = {1873-3468},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1016/S0014-5793%2899%2900346-4},
doi = {10/cvszx8},
abstract = {Purified barley leaf ADP-glucose pyrophosphorylase, a key enzyme of the starch synthesis in the chloroplast stroma, was analysed with respect to its possible regulation by factors defining the metabolic/effector status of the chloroplast during light and dark conditions. The enzyme required 3-phosphoglyceric acid for the maximal activity and was inhibited by inorganic phosphate. The optimal pH for the enzyme was at circa 7.0, regardless of the presence or absence of 3-phosphoglyceric acid, whereas the maximal activation by 3-phosphoglyceric acid was observed at pH 8.5 and higher. Changes in the concentration of Mg2+ and dithiothreitol had little or no effect on the enzymatic activity of AGPase. It has been directly demonstrated for the first time that a 3-phosphoglyceric acid/inorganic phosphate ratio, a crucial regulatory parameter, could be directly related to a defined activation state of the enzyme, allowing the prediction of a relative AGPase activity under given conditions. The predicted changes in the enzyme activity were directly correlated with earlier reported responses of starch levels to the 3-phosphoglyceric acid/inorganic phosphate ratio in chloroplasts. Consequences of this for the starch biosynthesis are discussed.},
language = {en},
number = {1},
urldate = {2021-11-08},
journal = {FEBS Letters},
author = {Kleczkowski, Leszek A},
year = {1999},
note = {\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793\%2899\%2900346-4},
keywords = {Allosteric effector, Light regulation, Photosynthesis, Starch synthesis},
pages = {153--156},
}
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The enzyme required 3-phosphoglyceric acid for the maximal activity and was inhibited by inorganic phosphate. The optimal pH for the enzyme was at circa 7.0, regardless of the presence or absence of 3-phosphoglyceric acid, whereas the maximal activation by 3-phosphoglyceric acid was observed at pH 8.5 and higher. Changes in the concentration of Mg2+ and dithiothreitol had little or no effect on the enzymatic activity of AGPase. It has been directly demonstrated for the first time that a 3-phosphoglyceric acid/inorganic phosphate ratio, a crucial regulatory parameter, could be directly related to a defined activation state of the enzyme, allowing the prediction of a relative AGPase activity under given conditions. The predicted changes in the enzyme activity were directly correlated with earlier reported responses of starch levels to the 3-phosphoglyceric acid/inorganic phosphate ratio in chloroplasts. 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