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Metabolism and Enzymology

Identification of the 64 Kilodalton Chloroplast Stromal Phosphoprotein as Phosphoglucomutase ¹

U.S. Department of Agriculture, Agricultural Research Service, University of Kentucky, Lexington, Kentucky 40546, Biochemistry Department, University of Kentucky, Lexington, Kentucky 40546, Department of Biochemistry and Genetics, The Connecticut Agricultural Experiment Station, New Haven, Connecticut 06504

Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with [-³²P]ATP decreased in the presence of Glc-6-P and Glc-1,6-P₂, but was stimulated by glucose. Two-dimensional gel electrophoresis following incubation of intact chloroplasts and stromal extracts with [-³²P]ATP, or incubation of stromal extracts and partially purified phosphoglucomutase (EC 2.7.5.1) with [³²P]Glc-1-P showed that the identical 64 kilodalton polypeptide was labeled. A 62 kilodalton polypeptide was phosphorylated by incubation of tobacco (Nicotiana sylvestris) stromal extracts with either [-³²P]ATP or [³²P]Glc-1-P. In contrast, an analogous polypeptide was not phosphorylated in extracts from a tobacco mutant deficient in plastid phosphoglucomutase activity. The results indicate that the 64 (or 62) kilodalton chloroplast stromal phosphoprotein is phosphoglucomutase.

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