Enzyme co-localization in pea leaf chloroplasts: glyceraldehyde-3-P dehydrogenase, triose-P isomerase, aldolase and sedoheptulose bisphosphatase
| Autor: | Andrew A. Carol, Louise E. Anderson, Nandita Gatla |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Chloroplasts
Fructose 1 6-bisphosphatase Fructose-bisphosphate aldolase Plant Science Isomerase Biochemistry chemistry.chemical_compound Fructose-Bisphosphate Aldolase Sedoheptulose-bisphosphatase biology Chemistry Aldolase B Aldolase A Peas Glyceraldehyde-3-Phosphate Dehydrogenases Cell Biology General Medicine Immunohistochemistry Molecular biology Phosphoric Monoester Hydrolases Plant Leaves stomatognathic diseases Chloroplast stroma Sedoheptulose biology.protein Triose-Phosphate Isomerase |
| Zdroj: | Photosynthesis Research. 83:317-328 |
| ISSN: | 1573-5079 0166-8595 |
| DOI: | 10.1007/s11120-005-0790-2 |
| Popis: | 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 CO(2) 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. |
| Databáze: | OpenAIRE |
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