Heat Stability of Maize Endosperm ADP-Glucose Pyrophosphorylase Is Enhanced by Insertion of a Cysteine in the N Terminus of the Small Subunit

ADP-glucose pyrophosphorylase (AGPase) is a key regulatory enzyme in starch biosynthesis. However, plant AGPases differ in several parameters, including spatial and temporal expression, allosteric regulation, and heat stability. AGPases of cereal endosperms are heat labile, while those in other tiss...

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Veröffentlicht in:	Plant physiology (Bethesda) 2005-12, Vol.139 (4), p.1625-1634
Hauptverfasser:	Linebarger, Carla R. Lyerly, Boehlein, Susan K, Sewell, Aileen K, Shaw, Janine, Hannah, L. Curtis
Format:	Artikel
Sprache:	eng
Schlagworte:	ADP-glucose pyrophosphorylase Amino Acid Motifs Amino Acid Sequence amino acid sequences Amino acids Biochemical Processes and Macromolecular Structures Biological and medical sciences Corn cysteine Cysteine - chemistry Disulfides Endosperm enzyme activity Enzyme Stability Enzymes Fundamental and applied biological sciences. Psychology Gels Glucose-1-Phosphate Adenylyltransferase - chemistry Glucose-1-Phosphate Adenylyltransferase - genetics Glucose-1-Phosphate Adenylyltransferase - metabolism Hot Temperature insertional mutagenesis Kinetics Metabolism Molecular Sequence Data Mutagenesis, Insertional Mutagenesis, Site-Directed nucleotidyltransferases Photosynthesis, respiration. Anabolism, catabolism plant biochemistry plant genetics Plant physiology and development plant proteins Plants Plants, Genetically Modified Protein Structure, Quaternary Protein Subunits Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Starches thermal stability Tubers Zea mays Zea mays - enzymology Zea mays - genetics
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