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First published online June 10, 2005; 10.1104/pp.105.060699

Plant Physiology 138:1552-1562 (2005)
© 2005 American Society of Plant Biologists

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BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

Purification and Characterization of Adenosine Diphosphate Glucose Pyrophosphorylase from Maize/Potato Mosaics1

Susan K. Boehlein, Aileen K. Sewell, Joanna Cross2, Jon D. Stewart and L. Curtis Hannah*

Department of Biochemistry and Molecular Biology (S.K.B., A.K.S.), Department of Chemistry (J.D.S.), and Program in Plant Molecular and Cellular Biology and Horticultural Sciences (J.C., L.C.H.), University of Florida, Gainesville, Florida 32611

Adenosine diphosphate glucose pyrophosphorylase (AGPase) catalyzes a rate-limiting step in starch biosynthesis. The reaction produces ADP-glucose and pyrophosphate from glucose-1-P and ATP. Investigations from a number of laboratories have shown that alterations in allosteric properties as well as heat stability of this enzyme have dramatic positive effects on starch synthesis in the potato (Solanum tuberosum) tuber and seeds of important cereals. Here, we report the characterization of purified recombinant mosaic AGPases derived from protein motifs normally expressed in the maize (Zea mays) endosperm and the potato tuber. These exhibit properties that should be advantageous when expressed in plants. We also present an in-depth characterization of the kinetic and allosteric properties of these purified recombinant AGPases. These data point to previously unrecognized roles for known allosteric effectors.

1 This work was supported by the National Science Foundation (grant nos. IBN–9316887, IBN–960416, IBN–9982626, IBN–0444031, and MCB–9420422 to L.C.H.), the U.S. Department of Agriculture Competitive Grants Program (grant nos. 94–37300–453, 95–00836, 95–37301–2080, 97–01964, 97–36306–4461, 98–01006, and 2000–01488 to L.C.H.), and the Florida Agricultural Experiment Station (Journal Series No. R–10624).

2 Present address: Institute of Biological Chemistry, Washington State University, Pullman, WA 99164–6340.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.060699.

* Corresponding author; e-mail hannah{at}ifas.ufl.edu; fax 352–392–6957.

Received February 3, 2005; returned for revision March 7, 2005; accepted March 13, 2005.




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