Results 121 to 130 of about 1,681 (166)
Some of the next articles are maybe not open access.
Analysis and Elucidation of Phosphoenolpyruvate Carboxylase in Cyanobacteria
The Protein Journal, 2015Phosphoenolpyruvate carboxylase (PEPC) a cytosolic enzyme of higher plants is also found in bacteria and cyanobacteria. Genetic and biochemical investigations have indicated that there are several isoforms of PEPC belonging to C3; C3/C4 and C4 groups but, the evolution of PEPC in cyanobacteria is not yet understood.
Ramamoorthy Rajalakshmi +5 more
openaire +3 more sources
Phosphoenolpyruvate carboxylase assay on polyacrylamide gels
Experientia, 1979A 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, 1973Abstract 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, 1992In 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
Phosphoenolpyruvate Carboxylase: An Enzymologist's View
Annual Review of Plant Physiology, 1982INTRODUCTION . PREPARATION AND ASSAY OF PEP CARBOXYLASE .. Assay . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. .. . . . . . . . . . . . . .. .. .. . . . .. . . .. .. . . . .. . .. .. . .. . . .. . . . . . . . .. . . . . . . . . . . . . . . . . . . Assay Conditions . . . . . . . . . . . . . . . . . . .
openaire +2 more sources
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[
Walker, Robert P. +3 more
openaire +4 more sources
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[
Walker, Robert P. +3 more
openaire +4 more sources
Requirement for Phosphoenolpyruvate Carboxylase in a Cyanobacterium
1990Although cyanobacteria are known to assimilate inorganic carbon by the C3 photosynthetic pathway, they also fix large amounts of carbon in the light as C4 acids (1). These C4 acids, primarily aspartate and malate, may represent as much as 20% of the total carbon fixed and have been shown to be the product of phosphoenolpyruvate (PEP) carboxylase [EC 4 ...
J. R. Coleman, I. Luinenburg
openaire +2 more sources
Modification of maize phosphoenolpyruvate carboxylase by tetranitromethane
Phytochemistry, 1992Abstract Maize leaf phosphoenolpyruvate carboxylase was completely and irreversibly inactivated by treatment with micromolar concentrations of tetranitromethane. The inactivation did not follow any of the known kinetic mechanisms. The inactivation resulted from the specific modification of one tyrosine residue per enzyme protomer, although sulphydryl
Anil S. Bhagwat, Gururaj B. Maralihalli
openaire +2 more sources
The regulation of phosphoenolpyruvate carboxylase in CAM plants
Trends in Plant Science, 2000Phosphoenolpyruvate carboxylase catalyses the primary assimilation of CO(2) in Crassulacean acid metabolism plants. It is activated by phosphorylation, and this plays a major role in setting the day-night pattern of metabolism in these plants. The key factor that controls the phosphorylation state of phosphoenolpyruvate carboxylase is the activity of ...
openaire +3 more sources
Phosphoenolpyruvate carboxylase from Acetobacter aceti
Archives of Microbiology, 1979In Acetobacter aceti growing on pyruvate as the only source of carbon and energy, oxaloacetate (OAA) is produced by a phosphoenolpyruvate (PEP) carboxylase (EC 4.1.1.31). The enzyme was purified 122-fold and a molecular weight of about 380,000 was estimated by gel filtration.
J. P. Schwitzguébel, L. Ettlinger
openaire +2 more sources