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Since plant phosphoenolpyruvate carboxylase (PEPC) was last reviewed in the Annual Review of Plant Physiology over a decade ago (O’Leary 1982), significant advances have been made in our knowledge of this oligomeric, cytosolic enzyme. This review highlights this exciting progress in plant PEPC research by focusing on the three major areas of recent(More)
Substrate ribulose bisphosphate is a potent and a weak inhibitor of the rate of CO2/Mg2+ activation in the carboxylase purified from spinach leaves and Rhodospirillum rubrum, respectively. At 2 degrees C, the concentration of ribulose bisphosphate required for 50% inhibition of the initial rate of CO2/Mg2+ activation was less than 0.4 microM for the spinach(More)
Control of C(4) photosynthesis and Crassulacean acid metabolism (CAM) is, in part, mediated by the diel regulation of phosphoenolpyruvate carboxylase (PEPC) activity. The nature of this regulation of PEPC in the leaf cell cytoplasm of C(4) and CAM plants is both metabolite-related and posttranslational. Specificially, the regulatory properties of the enzyme(More)
The phosphoenolpyruvate (PPrv) carboxylase isozyme involved in C4 photosynthesis undergoes a day/night reversible phosphorylation process in leaves of the C4 plant, Sorghum. Ser8 of the target enzyme oscillates between a high (light) and a low (dark) phosphorylation status. Both in vivo and in vitro, phosphorylation of dark-form carboxylase was accompanied(More)
Phosphoenolpyruvate carboxylase (PEPCase) from light- and dark-adapted maize leaves was rapidly purified in the presence of L-malate and glycerol to apparent electrophoretic homogeneity by ammonium sulfate fractionation, hydroxylapatite chromatography, and fast-protein liquid chromatography on Mono Q. The resulting preparations were totally devoid of(More)
We have recently reported that the light-induced changes in the enzymatic and regulatory properties of maize leaf phosphoenolpyruvate carboxylase are attributed to the regulatory seryl phosphorylation of this C4-photosynthesis enzyme. In the present study, the darkform target enzyme was phosphorylated/activated in vitro by a maize leaf protein-serine(More)
The distribution of (14)C in photosynthetic metabolites of two naturally occurring higher plants with reduced photorespiration, Moricandia arvensis and Panicum milioides, in pulse and pulse-chase (14)CO(2) incorporation experiments was similar to that for the C(3) species, M. foetida and Glycine max. After 6 seconds of (14)CO(2) incorporation, only about 6%(More)
Flaveria cronquistii (C(3)), F. chloraefolia (C(3)-C(4)), F. floridana (C(3)-C(4)), F. pubescens (C(3)-C(4)), F. anomala (C(3)-C(4)), F. linearis (C(3)-C(4)), F. brownii (C(4)), F. palmeri (C(4)), F. trinervia (C(4)) and F. australasica (C(4)), comprising 10 out of the 21 known species of the genus Flaveria (Asteraceae), were included in a comparative study(More)
Plant phosphoenolpyruvate carboxylase (PEPc) activity and allosteric properties are regulated by PEPc kinase (PPcK) through reversible phosphorylation of a specific serine (Ser) residue near the N terminus. We report the molecular cloning of PPcK from the facultative Crassulacean acid metabolism (CAM) common ice plant (Mesembryanthemum crystallinum), using(More)
The active site(s) of the bifunctional regulatory protein of pyruvate,orthophosphate dikinase catalyze(s) the Pi-dependent activation (dephosphorylation) and ADP-dependent inactivation (phosphorylation) of maize leaf dikinase. The chemical modification studies of the regulatory protein active sites presented in this paper are interpreted as showing the two(More)