Inhibition of Escherichia coli inorganic pyrophosphatase by fructose-1-phosphate
- Authors: Vorobyeva N.N.1,2, Kurilova S.A.2, Anashkin V.A.2, Rodina E.V.1
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Affiliations:
- Faculty of Chemistry
- Belozersky Institute of Physico-Chemical Biology
- Issue: Vol 82, No 8 (2017)
- Pages: 953-956
- Section: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/151457
- DOI: https://doi.org/10.1134/S0006297917080107
- ID: 151457
Cite item
Abstract
Pyrophosphate regulates vital cellular reactions, and its level in E. coli cells is under the ultimate control of inorganic pyrophosphatase. The mechanisms involved in the regulation of pyrophosphatase activity still need to be elucidated. The present study demonstrated that fructose-1-phosphate inhibits pyrophosphatase activity by a mechanism not involving competition with substrate for binding to the active site. The inhibition constant governing the binding of the inhibitor to the enzyme–substrate complex is 1.1 mM. Substitutions of Lys112, Lys115, Lys148, and Arg43 in the regulatory site completely or partially abolished the inhibition. Thus, Fru-1-P is a physiological inhibitor of pyrophosphatase that acts via a regulatory site in this enzyme.
About the authors
N. N. Vorobyeva
Faculty of Chemistry; Belozersky Institute of Physico-Chemical Biology
Author for correspondence.
Email: nvorob@yandex.ru
Russian Federation, Moscow, 119991; Moscow, 119991
S. A. Kurilova
Belozersky Institute of Physico-Chemical Biology
Email: nvorob@yandex.ru
Russian Federation, Moscow, 119991
V. A. Anashkin
Belozersky Institute of Physico-Chemical Biology
Email: nvorob@yandex.ru
Russian Federation, Moscow, 119991
E. V. Rodina
Faculty of Chemistry
Email: nvorob@yandex.ru
Russian Federation, Moscow, 119991
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