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Purification and characterization of adenosine diphosphate glucose pyrophosphorylase from maize/potato mosaics
被引:29
作者:
Boehlein, SK
Sewell, AK
Cross, J
Stewart, JD
Hannah, LC
[1
]
机构:
[1] Univ Florida, Program Plant Mol & Cellular Biol & Hort Sci, Gainesville, FL 32611 USA
[2] Univ Florida, Dept Biochem & Mol Biol, Gainesville, FL 32611 USA
[3] Univ Florida, Dept Chem, Gainesville, FL 32611 USA
关键词:
D O I:
10.1104/pp.105.060699
中图分类号:
Q94 [植物学];
学科分类号:
071001 ;
摘要:
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.
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页码:1552 / 1562
页数:11
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