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- W81596586 abstract "SummaryC4 species have a specific isoform of phosphoenolpyruvate Carboxylase (PEPC) that catalyzes primary CO2 fixation in the C4 photosynthesis pathway. It has long been known that the enzyme in the cytosol of the mesophyll cells is subject to allosteric control by opposing photosynthesis-related metabolites. The discovery of a phosphorylation process acting on C4 PEPC, via a complex light-signal transduction cascade, has revitalized interest in this enzyme and the ensuing wealth of data has highlighted one of a few signaling cascades known so far in the regulation of plant metabolism. The cascade depends upon a cross-talk between the two neighboring photosynthetic cell types, involves classical second messengers like pH, Inosital-1,4 5-trisphosphate (Ins(1,4,5) P3) and calcium, and upregulates the activity of a Ca2+-independent, C4 PEPC-specific protein-serine/threonine kinase, which finally phosphorylates PEPC. The final activity of C4 PEPC and the resulting carbon flux to bundle sheath cells are dependent on the mutual interaction between metabolite and covalent control mechanisms acting on this enzyme." @default.
- W81596586 created "2016-06-24" @default.
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- W81596586 date "2006-03-01" @default.
- W81596586 modified "2023-09-30" @default.
- W81596586 title "Reversible Phosphorylation in the Regulation of Photosynthetic Phosphoenolpyruvate Carboxylase in C4 Plants" @default.
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- W81596586 doi "https://doi.org/10.1007/0-306-48148-0_21" @default.
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