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Inhibition of Sucrose:Sucrose Fructosyl Transferase by Cations and Ionic Strength

Inhibition of Sucrose:Sucrose Fructosyl Transferase by Cations and Ionic Strength Abstract Fructans are storage carbohydrates found in many temperate grasses. The first enzyme in the biosynthetic pathway of most fructans is sucrose:sucrose fructosyl transferase (SST). In this report, we demonstrate that K+ and ionic strength noncompetitively inhibit the activity of SST from wheat (Triticum aestivum L.) stems. The Ki for this inhibition is high, 122 mM, but in the range of concentrations of K+ found in the tissue (205–)314 mM). Addition of KCl to the assay system had no effect on the pH optimum (5.5) or the Km for sucrose (266 mM) but reduced the Vmax. At equivalent ionic strengths, inhibition by choline chloride was about half that of KCl, indicating that inhibition by ionic strength might be responsible for approximately 50% of the KCl inhibition. Inhibition by LiCl and (NH4)2SO4 was similar to that by choline chloride. Soluble invertase activity found in the SST preparations was less sensitive to KCl and more sensitive to choline chloride than was SST. SST from barley (Hordeum vulgare L.) stems and leaves, as well as SST from leaves of orchardgrass (Dactylis glomerata), was also inhibited by KCl. SST from onion (Allium cepa L.) bulbs and asparagus (Asparagus officinalis L.) stems was not inhibited by KCl; thus, inhibition of activity by KCl is not a universal characteristic of SST from all sources. This content is only available as a PDF. Copyright © 1993 by American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model) http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Physiology Oxford University Press

Inhibition of Sucrose:Sucrose Fructosyl Transferase by Cations and Ionic Strength

Chevalier, P. M.; Rupp, R. A.
Plant Physiology , Volume 101 (2) – Feb 1, 1993
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References (18)

Publisher
Oxford University Press
Copyright
Copyright © 2021 American Society of Plant Biologists
ISSN
0032-0889
eISSN
1532-2548
DOI
10.1104/pp.101.2.589
Publisher site
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Abstract

Abstract Fructans are storage carbohydrates found in many temperate grasses. The first enzyme in the biosynthetic pathway of most fructans is sucrose:sucrose fructosyl transferase (SST). In this report, we demonstrate that K+ and ionic strength noncompetitively inhibit the activity of SST from wheat (Triticum aestivum L.) stems. The Ki for this inhibition is high, 122 mM, but in the range of concentrations of K+ found in the tissue (205–)314 mM). Addition of KCl to the assay system had no effect on the pH optimum (5.5) or the Km for sucrose (266 mM) but reduced the Vmax. At equivalent ionic strengths, inhibition by choline chloride was about half that of KCl, indicating that inhibition by ionic strength might be responsible for approximately 50% of the KCl inhibition. Inhibition by LiCl and (NH4)2SO4 was similar to that by choline chloride. Soluble invertase activity found in the SST preparations was less sensitive to KCl and more sensitive to choline chloride than was SST. SST from barley (Hordeum vulgare L.) stems and leaves, as well as SST from leaves of orchardgrass (Dactylis glomerata), was also inhibited by KCl. SST from onion (Allium cepa L.) bulbs and asparagus (Asparagus officinalis L.) stems was not inhibited by KCl; thus, inhibition of activity by KCl is not a universal characteristic of SST from all sources. This content is only available as a PDF. Copyright © 1993 by American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Journal

Plant Physiology – Oxford University Press

Published: Feb 1, 1993

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