First published online June 10, 2005; 10.1104/pp.105.060699
Plant Physiology 138:1552-1562 (2005)
© 2005 American Society of Plant Biologists
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.
This article has been cited by other articles:
|
|
|
|
 
S. K. Boehlein, J. R. Shaw, J. D. Stewart, and L. C. Hannah
Studies of the Kinetic Mechanism of Maize Endosperm ADP-Glucose Pyrophosphorylase Uncovered Complex Regulatory Properties
Plant Physiology,
February 1, 2010;
152(2):
1056 - 1064.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. K. Boehlein, J. R. Shaw, L. C. Hannah, and J. D. Stewart
Probing Allosteric Binding Sites of the Maize Endosperm ADP-Glucose Pyrophosphorylase
Plant Physiology,
January 1, 2010;
152(1):
85 - 95.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. L. Kuhn, C. A. Falaschetti, and M. A. Ballicora
Ostreococcus tauri ADP-glucose Pyrophosphorylase Reveals Alternative Paths for the Evolution of Subunit Roles
J. Biol. Chem.,
December 4, 2009;
284(49):
34092 - 34102.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
N. Georgelis, J. R. Shaw, and L. C. Hannah
Phylogenetic Analysis of ADP-Glucose Pyrophosphorylase Subunits Reveals a Role of Subunit Interfaces in the Allosteric Properties of the Enzyme
Plant Physiology,
September 1, 2009;
151(1):
67 - 77.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. K. Boehlein, J. R. Shaw, J. D. Stewart, and L. C. Hannah
Characterization of an Autonomously Activated Plant ADP-Glucose Pyrophosphorylase
Plant Physiology,
January 1, 2009;
149(1):
318 - 326.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. K. Boehlein, J. R. Shaw, J. D. Stewart, and L. C. Hannah
Heat Stability and Allosteric Properties of the Maize Endosperm ADP-Glucose Pyrophosphorylase Are Intimately Intertwined
Plant Physiology,
January 1, 2008;
146(1):
289 - 299.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
N. Georgelis, E. L. Braun, J. R. Shaw, and L. C. Hannah
The Two AGPase Subunits Evolve at Different Rates in Angiosperms, yet They Are Equally Sensitive to Activity-Altering Amino Acid Changes When Expressed in Bacteria
PLANT CELL,
May 1, 2007;
19(5):
1458 - 1472.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. A. Iglesias, M. A. Ballicora, J. I. Sesma, and J. Preiss
Domain Swapping between a Cyanobacterial and a Plant Subunit ADP-Glucose Pyrophosphorylase
Plant Cell Physiol.,
April 1, 2006;
47(4):
523 - 530.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
C. R. L. Linebarger, S. K. Boehlein, A. K. Sewell, J. Shaw, and L. C. Hannah
Heat Stability of Maize Endosperm ADP-Glucose Pyrophosphorylase Is Enhanced by Insertion of a Cysteine in the N Terminus of the Small Subunit
Plant Physiology,
December 1, 2005;
139(4):
1625 - 1634.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
