Results 231 to 240 of about 60,616 (293)
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Phosphorylation of phosphoenolpyruvate carboxykinase (PEPCK) and phosphoenolpyruvate carboxylase (PEPC) in the flesh of fruits.

Plant Physiology and Biochemistry, 2016
This study determined whether phosphoenolpyruvate carboxykinase (PEPCK) and phosphoenolpyruvate carboxylase (PEPC) are phosphorylated in the flesh of a range of fruits. This was done by incubating fruit flesh with 32P[P] (where 32P[P] = 32PO43-), then PEPCK and PEPC were immunoprecipitated from extracts using specific antisera. The incorporation of 32P[
R. P. Walker   +3 more
semanticscholar   +5 more sources

Evolution of C4 phosphoenolpyruvate carboxylase

Archives of Biochemistry and Biophysics, 2003
C4 plants are known to be of polyphyletic origin and to have evolved independently several times during the evolution of angiosperms. This implies that the C4 isoform of phosphoenolpyruvate carboxylase (PEPC) originated from a nonphotosynthetic PEPC gene that was already present in the C3 ancestral species.
Peter Westhoff   +2 more
openaire   +3 more sources

Nodule phosphoenolpyruvate carboxylase: a review

Physiologia Plantarum, 1988
Recent data concerning the fixation of CO2 and the functioning of phosphoenolpyruvate (PEP) carboxylase (EC 4.1.1.31) in legume, nodules are reviewed. The activites of N2 fixation (acctylene reduction) and PEP carboxylase are correlated Activities of PEP carboxylase are always higher in nodules than in roots.
Deroche, M.E., Carrayol, E.
openaire   +3 more sources

Effect of LiCl on phosphoenolpyruvate carboxylase kinase and the phosphorylation of phosphoenolpyruvate carboxylase in leaf disks and leaves of Sorghum vulgare [PDF]

open access: possiblePlanta, 2006
In the present work, the effect of LiCl on phosphoenolpyruvate carboxylase kinase (PEPCase-k), C4 phosphoenolpyruvate carboxylase (PEPCase: EC 4.1.1.31) and its phosphorylation process has been investigated in illuminated leaf disks and leaves of the C4 plant Sorghum vulgare.
Sofía García-Mauriño   +4 more
openaire   +2 more sources

Phosphoenolpyruvate carboxylase: structure, regulation and evolution

Plant Science, 1994
Abstract Plant phosphoenolpyruvate carboxylase (EC 4.1.1.31; PEPC) is encoded by a small multigene family in which the expression of each member is controlled individually by exogenous (light, environmental) and/or endogenous (hormonal and developmental) stimuli.
Lepiniec, Loic   +4 more
openaire   +3 more sources

The unique phosphoenolpyruvate carboxylase kinase

Plant Physiology and Biochemistry, 2003
Abstract This paper deals with the contribution of P. Gadal’s group to the study of the phosphoenolpyruvate carboxylase protein kinase. It traces the important steps from the discovery up to the present time leading to characterize a new protein kinase which is specific for plants and displays original properties.
Jean Vidal, Cristina Echevarría
openaire   +2 more sources

Phosphoenolpyruvate carboxylase regulation in C4-PEPC-expressing transgenic rice during early responses to drought stress.

Physiologia Plantarum : An International Journal for Plant Biology, 2017
Phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) has important functions in C4 photosynthesis and biosynthesis of intermediate metabolites. In this study, the drought resistance of C4-PEPC-expressing transgenic rice (Oryza sativa, line PC) plants was ...
Xiaolong Liu   +6 more
semanticscholar   +1 more source

Phosphoenolpyruvate carboxylase assay on polyacrylamide gels

Experientia, 1979
A simple technique to identify, PEP carboxylase on polyacrylamide gels is described. This method involves in the formation of white ring of calcium phosphate precipitate on the reaction site, revealing the presence of enzyme protein.
K. Francis, A. Gnanam
openaire   +3 more sources

A procedure for the electrophoretic analysis of phosphoenolpyruvate carboxylase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1973
Abstract Phosphoenolpyruvate carboxylase from Euglena gracilis was analyzed electrophoretically using an agar suspension of the reaction mixture to detect the enzyme bands. Since the stain is specific for oxaloacetate produced by the enzyme, it should be possible to extend this technique to other enzymes concerned with oxaloacetate metabolism.
Robert C. Karn   +2 more
openaire   +3 more sources

Hydrolysis of phosphoenolpyruvate catalyzed by phosphoenolpyruvate carboxylase from Zea mays

Biochemistry, 1992
In addition to the normal carboxylation reaction, phosphoenolpyruvate carboxylase from Zea mays catalyzes a HCO3(-)-dependent hydrolysis of phosphoenolpyruvate to pyruvate and Pi. Two independent methods were used to establish this reaction. First, the formation of pyruvate was coupled to lactate dehydrogenase in assay solutions containing high ...
Scott L. Ausenhus, Marion H. O'Leary
openaire   +3 more sources

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