Inhibition of Escherichia coli inorganic pyrophosphatase by fructose-1-phosphate


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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.

作者简介

N. Vorobyeva

Faculty of Chemistry; Belozersky Institute of Physico-Chemical Biology

编辑信件的主要联系方式.
Email: nvorob@yandex.ru
俄罗斯联邦, Moscow, 119991; Moscow, 119991

S. Kurilova

Belozersky Institute of Physico-Chemical Biology

Email: nvorob@yandex.ru
俄罗斯联邦, Moscow, 119991

V. Anashkin

Belozersky Institute of Physico-Chemical Biology

Email: nvorob@yandex.ru
俄罗斯联邦, Moscow, 119991

E. Rodina

Faculty of Chemistry

Email: nvorob@yandex.ru
俄罗斯联邦, Moscow, 119991


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