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Enzyme co-localization in pea leaf chloroplasts: glyceraldehyde-3-P dehydrogenase,triose-P isomerase,aldolase and sedoheptulose bisphosphatase
Authors:Email author" target="_blank">Louise?E?AndersonEmail author  Nandita?Gatla  Andrew?A?Carol
Institution:(1) Department of Biological Sciences, University of Illinois-Chicago, 845 West Taylor, IL Chicago, 60607, USA
Abstract:Nearest neighbor analysis of immunocytolocalization experiments indicates that the enzymes glyceraldehyde-3-P dehydrogenase, triose-P isomerase and aldolase are located close to one another in the pea leaf chloroplast stroma, and that aldolase is located close to sedoheptulose bisphosphatase. Direct transfer of the triose phosphates between glyceraldehyde-3-P dehydrogenase and triose-P isomerase, and from glyceraldehyde-3-P dehydrogenase and triose-P isomerase to aldolase, is then a possibility, as is direct transfer of sedoheptulose bisphosphate from aldolase to sedoheptulose bisphosphatase. Spatial organization of these enzymes may be important for efficient CO2 fixation in photosynthetic organisms. In contrast, there is no indication that fructose bisphosphatase is co-localized with aldolase, and direct transfer of fructose bisphosphate from aldolase to fructose bisphosphatase seems unlikely.
Keywords:aldolase  enzyme co-localization  fructose bisphosphatase  functional enzyme complexes  glyceraldehyde-3-P dehydrogenase          Pisum sativum          photosynthetic CO2-fixation  sedoheptulose bisphosphatase  spatial organization of Calvin cycle enzymes in the chloroplast  triose-P isomerase
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