Activation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxin

Miguel A. Ballicora, Jeremiah B. Frueauf, Yingbin Fu, Peter Schürmann, Jack Preiss

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130 Scopus citations


The potato tuber (Solanum tuberosum L.) ADP-glucose pyrophosphorylase (ADP-GlcPPase) catalyzes the first committed step in starch biosynthesis. The main type of regulation of this enzyme is allosteric, and its activity is controlled by the ratio of activator, 3-phosphoglycerate to inhibitor, P(i). It was reported (Fu, Y., Ballicora, M. A., Leykam, J. F., and Preiss, J. (1998) J. Biol. Chem. 273, 25045-25052) that the enzyme was activated by reduction of the Cys12 disulfide linkage present in the catalytic subunits. In this study, both reduced thioredoxin f and m from spinach (Spinacia oleracea) leaves reduced and activated the enzyme at low concentrations (10 μM) of activator (3-phosphoglycerate). Fifty percent activation was at 4.5 and 8.7 μM for reduced thioredoxin f and m, respectively, and 2 orders of magnitude lower than for dithiothreitol. The activation was reversed by oxidized thioredoxin. Cys12 is conserved in the ADP-GlcPPases from plant leaves and other tissues except for the monocot endosperm enzymes. We postulate that in photosynthetic tissues, reduction could play a role in the fine regulation of the ADP-GlcPPase mediated by the ferredoxin-thioredoxin system. This is the first time that a covalent mechanism of regulation is postulated in the synthesis of starch.

Original languageEnglish (US)
Pages (from-to)1315-1320
Number of pages6
JournalJournal of Biological Chemistry
Issue number2
StatePublished - Jan 14 2000

ASJC Scopus subject areas

  • Biochemistry


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