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GrainGenes Reference Report: PPS-121-965

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Reference	PPS-121-965
Title	The allosterically unregulated isoform of ADP-glucose pyrophosphorylase from barley endosperm is the most likely source of ADP-glucose incorporated into endosperm starch
Journal	Plant Physiology
Year	1999
Volume	121
Pages	965-975
Author	Doan DNP Rudi H Olsen OA
Abstract	Summary: We present the results of studies of an unmodified version of the recombinant major barley (Hordeum vulgare) endosperm ADP-glucose pyrophoshorylase (AGPase) expressed in insect cells, which corroborate previous data that this isoform of the enzyme acts independently of the allosteric regulators 3-phosphoglycerate and inorganic phosphate. We also present a characterization of the individual subunits expressed separately in insect cells, showing that the SS AGPase is active in the presence of 3-phosphoglycerate and is inhibited by inorganic phosphate. As a step toward the elucidation of the role of the two AGPase isoforms in barley, the temporal and spatial expression profile of the four barley AGPase transcripts encoding these isoforms were studied. The results show that the steady-state level of beps and bepl, the transcripts encoding the major endosperm isoform, correlated positively with the rate of endosperm starch accumulation. In contrast, blps and blpl, the transcripts encoding the major leaf isoform, were constitutively expressed at a very low steady-state level throughout the barley plant. The implications of these findings for the evolution of plant AGPases are discussed
Keyword	[ Hide all but 1 of 28 ] adenosine phosphates adp glucose pyrophosphorylase barley barley endosperm carbohydrate metabolism cell cell culture complementary dna endosperm endosperm starch enzyme evolution gene expression glycerate 3 phosphate hordeum vulgare insect isoenzyme isoforms messenger rna phosphate protein synthesis recombinant proteins regulation regulators spodoptera frugiperda starch transcript transgenics

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