FEBS Letters · 2000 · 16 citations · 30 references
Life SciencesBiochemistryCell BiologyCarbohydrate BiochemistryCellular MetabolismEnzymologyCarbohydrate MetabolismCell Wall BiosynthesisCarbohydrate-active EnzymesFractionationStarch Metabolism EnzymesSubcellular Fractionation
The intracellular localizations of ADPglucose pyrophosphatase (AGPPase) and ADPglucose pyrophosphorylase (AGPase) have been studied using protoplasts prepared from suspension-cultured cells of sycamore (Acer pseudoplatanus L.). Subcellular fractionation studies revealed that all the AGPPase present in the protoplasts is associated with amyloplasts, whereas more than 60% of AGPase is in the extraplastidial compartment. Immunoblots of amyloplast- and extraplastid-enriched extracts further confirmed that AGPase is located mainly outside the amyloplast. Experiments carried out to identify possible different isoforms of AGPPase in the amyloplast revealed the presence of soluble and starch granule-bound isoforms. We thus propose that ADPglucose levels linked to starch biosynthesis in sycamore cells are controlled by enzymatic reactions catalyzing the synthesis and breakdown of ADPglucose, which take place both inside and outside the amyloplast.
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Conservation and Duplication of Isozymes in Plants
L. D. Gottlieb · Science · 1982 · 614 citations
Hydrolytic Enzymes in the Central Vacuole of Plant Cells
Thomas Boller, Hans Kende · PLANT PHYSIOLOGY · 1979 · 505 citations · Full text
The Major Form of ADP-Glucose Pyrophosphorylase in Maize Endosperm Is Extra-Plastidial
Kay Denyer, F. Dunlap, Patrick J. Keeling et al. · PLANT PHYSIOLOGY · 1996 · 291 citations · Full text