Abstract
Near-full-length cDNA clones to the small and large subunit of the heterotetrameric potato tuber ADP-glucose pyrophosphorylase have been isolated and characterized. The missing amino terminal sequence of the small subunit has also been elucidated from its corresponding genomic clone. Primary sequence comparisons revealed that each potato subunit had less identity to each other than to their homologous subunit from other plants. It also appeared that the smaller subunit is more conserved among the different plants and the larger subunit more divergent. Amino acid comparisons of both potato tuber sequences to the Escherichia coli ADP-glucose pyrophosphorylase sequence revealed conserved regions important for both catalytic and allosteric function of the bacterial enzyme.
MeSH Terms
Amino Acid Sequence
Cloning, Molecular
DNA/genetics,isolation & purification
Escherichia coli/enzymology,genetics
Glucose-1-Phosphate Adenylyltransferase
Macromolecular Substances
Molecular Sequence Data
Nucleotidyltransferases/genetics
Plants/enzymology,genetics
Sequence Homology, Nucleic Acid
Solanum tuberosum/enzymology,genetics
Chemicals
Macromolecular Substances
DNA
Nucleotidyltransferases
Glucose-1-Phosphate Adenylyltransferase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Nakata P A
Program in Biochemistry and Biophysics, Washington State University, Pullman 99164-6340.
Greene T W
Anderson J M
Smith-White B J
Okita T W
Preiss J
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