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Involvement of Ubiquitin in Phosphoenolpyruvate Carboxylase Degradation
Botanica Acta, 1993AbstractWestern immunoblot analysis of protein extracts prepared from epidermal peels, whole leaves, and mesophyll protoplasts with ubiquitin and PEPCase antibodies indicated ubiquitinated PEPCase bands and degradation products only in crude extracts which have been obtained in the presence of the proteolysis inhibitors leupeptin and hemin.
Heide Schnabl +3 more
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Chapter 13 C4-Phosphoenolpyruvate Carboxylase [PDF]
, 2010 Phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) is one of the enzymes indispensable for all variants of the C4 photosynthetic pathway. C4 photosynthesis evolved polyphyletically implying that the genes encoding the C4 PEPC originated several times independently from non-photosynthetic ancestral genes.
Peter Westhoff, Udo Gowik
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The mechanism of inhibition of phosphoenolpyruvate carboxylase by quinolinic acid
Biochimica et Biophysica Acta (BBA) - Enzymology, 1972Abstract The effect of quinolinic acid and its ferrous and manganous derivatives on phosphoenolpyruvate (PEP) carboxylase (GTP:oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.32) from rat liver cytoplasm is dependent upon the concentration of oxaloacetate in the assay system.
H.G. McDaniel +2 more
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In vivo phosphorylation of sorghum leaf phosphoenolpyruvate carboxylase
Biochimie, 1988The use of immunological techniques allowed us to purify close to homogeneity phosphoenolpyruvate carboxylase (PEPc, EC 4.1.1.31) from sorghum leaf. It was thus established that: 1) this protein is phosphorylated in vivo on seryl residues; 2) in C4-type photosynthesis, the phosphorylation process mainly concerns the PEPC isozyme form G; 3) enzyme ...
René Rémy +5 more
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A microtiter plate-based assay for phosphoenolpyruvate carboxylase
Analytical Biochemistry, 1990A sensitive, quantitative assay for phosphenolpyruvate carboxylase which utilizes microtiter plates is described. The assay depends upon the production of a colored compound in the reaction between oxaloacetate, the product of the phosphoenolpyruvate reaction, and the dye Fast Violet B.
Stephen P. Slocombe +7 more
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Phosphoenolpyruvate carboxylase and ammonium metabolism in oral streptococci
Archives of Oral Biology, 1973Abstract Oral streptococci were grown in media which provide various nitrogen sources. Ammonium fixation was studied in cell-free extracts of the cells. Carbon dioxide fixation was studied in washed intact cells and in crude and partially purified extracts of the cells.
Jan Carlsson, Tadashi Yamada
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Effects of pH on inactivation of maize phosphoenolpyruvate carboxylase
Archives of Biochemistry and Biophysics, 1990Maize leaf phosphoenolpyruvate carboxylase (PEPC) is inactivated by incubation at pH's above neutrality. Both the amount and the rapidity of inactivation increase as the pH rises. The presence of phosphoenolpyruvate (PEP), malate, glucose 6-phosphate and dithiothreitol in the incubation medium give protection to the enzyme.
Randolph T. Wedding, M. K. Black
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Quantitative Immunochemistry of Plant Phosphoenolpyruvate Carboxylases
1986Since its discovery (Bandurski and Greiner 1953) phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) has attracted increasing interest among plant scientists. The enzyme catalyses the reaction of CO3H− and phosphoenolpyruvate to produce oxaloacetate, immediately reduced to form malate; this latter can be oxidatively decarboxylated by NADP malic enzyme,
J. Brulfert, J. Vidal
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Sheep kidney phosphoenolpyruvate carboxylase purification and properties
Biochimica et Biophysica Acta (BBA) - Enzymology, 1972Phosphoenolpyruvate carboxylase (GTP: oxaloacetate carboxy-lase (transphosphorylating), EC 4.1.1.32) has been purified and obtained in a homogeneous form from sheep kidney cortex mitochondria. The purification procedure involved extraction of the freeze-dried mitochondria, (NH4)2SO4 fractionation, Sephadex G-100 gel filtration and ion-exchange ...
R.J. Barns, D.B. Keech
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On the cellular localization of phosphoenolpyruvate carboxylase in Sorghum leaves
Planta, 1981The localization of phosphoenol pyruvate carboxylase (EC 4.1.1.3.1.) in the leaf cells of Sorghum vulgare was investigated by using three techniques: the conventional aqueous and non aqueous methods gave conflicting results; the immunocytochemical techniques clearly showed that the enzyme is predominantly located in the cytoplasm of mesophyll cells.
Jean Vidal +3 more
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