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Phosphorylation of Phosphoenolpyruvate carboxylase is not essential fo high photosynthetic rates in the C4 species laveria bidentis 1[OA]

Furumoto, Tsuyoshi; Izui, Katsura; Quinn, Vanda; Furbank, Robert Thomas; von Caemmerer, Susanne


Phosphoenolpyruvate carboxylase (PEPC; EC4.1.1.31) plays a key role during C4 photosynthesis. The enzyme is activated by metabolites such as glucose-6-phosphate and inhibited by malate. This metabolite sensitivity is modulated by the reversible phosphorylation of a conserved serine residue near the N terminus in response to light. The phosphorylation of PEPC is modulated by a protein kinase specific to PEPC (PEPC-PK). To explore the role PEPC-PK plays in the regulation of C4 photosynthetic CO2...[Show more]

CollectionsANU Research Publications
Date published: 2007
Type: Journal article
Source: Plant Physiology
DOI: 10.1104/pp.107.102541


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