Results 231 to 240 of about 25,845 (262)
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Multiple forms of phosphoenolpyruvate carboxylase from Chlamydomonas reinhardtii
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1970Abstract 1. 1. Two species of phosphoenolpyruvate carboxylase (orthophosphate: oxalacetate carboxylase (phosphorylating), EC 4.1.1.31), have been isolated and purified from Chlamydomonas reinhardtii by salt fractionation, ion exchange chromatography on DEAE-cellulose, and by hydroxylapatite chromatography. 2. 2.
J H, Chen, R F, Jones
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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 ...
M T, Guidici-Orticoni +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.
W, Cockburn +3 more
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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.
Mohandass, Shylajanaciyar +5 more
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[45] Phosphoenolpyruvate carboxylase from Escherichia coli
1969Publisher Summary The chapter describes the purification procedure and properties of phosphoenolpyruvate carboxylase. The method is used for the purification of the enzyme from E. coli strain W, grown aerobically at 30° on a medium containing 50 mM glycerol as carbon source.
J.L. Cánovas, H.L. Kornberg
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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.
T, Yamada, J, Carlsson
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Nucleotide regulation of phosphoenolpyruvate carboxylase from Escherichia coli
Archives of Biochemistry and Biophysics, 1976Abstract Adenine, cytosine, guanine, and uracil nucleotides were surveyed as possible modulators of Escherichia coli phosphoenolpyruvate carboxylase. CMP, CDP, CTP, GDP, and GTP activate, ATP and GMP inhibit. The other nucleotides are without effect. Nucleotide activation is synergistic with acetyl-CoA or laurate.
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Escherichia coli phosphoenolpyruvate carboxylase: Characterization and sedimentation behavior
Archives of Biochemistry and Biophysics, 1968Abstract Phosphoenolpyruvate (PEP) carboxylase was partially purified from extracts of Escherichia coli . Sedimentation analyses of the enzyme in sucrose gradients indicate association-dissociation reactions involving monomeric units of 94,000 molecular weight.
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[Pyruvate and phosphoenolpyruvate carboxylase in methylotrophs].
Mikrobiologiia, 1979The activity of pyruvate and phosphoenolpyruvate carboxylases was determined in cell extracts of obligate and facultative methylotrophs which metabolized monocarbon reduced compounds via different pathways. Phosphoenolpyruvate carboxylase was found to be the only enzyme responsible for the high level of CO2 fixation by methylotrophs with the serine ...
N B, Loginova, Iu A, Trotsenko
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A new-to-nature carboxylation module to improve natural and synthetic CO2 fixation
Nature Catalysis, 2021Thomas Beneyton +2 more
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