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J Biol Chem, Vol. 275, Issue 2, 1315-1320, January 14, 2000

Activation of the Potato Tuber ADP-glucose Pyrophosphorylase by Thioredoxin*

Miguel A. Ballicora, Jeremiah B. Frueauf, Yingbin FuDagger , Peter Schürmann§, and Jack Preiss

From the Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824 and the § Laboratoire de Biochimie, Université de Neuchâtel, Neuchâtel CH-2007, Switzerland

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, Pi. 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.

* This work was supported in part by Department of Energy Grant DE-FG02-93ER20121.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Dept. of Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, MD 21205.

To whom correspondence should be addressed. Tel.: 517-353-3137; Fax: 517-353-9334; E-mail: preiss@pilot.msu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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