Results 241 to 250 of about 60,616 (293)

Phosphoenolpyruvate Carboxylase: An Enzymologist's View

Annual Review of Plant Physiology, 1982
INTRODUCTION . PREPARATION AND ASSAY OF PEP CARBOXYLASE .. Assay . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. .. . . . . . . . . . . . . .. .. .. . . . .. . . .. .. . . . .. . .. .. . .. . . .. . . . . . . . .. . . . . . . . . . . . . . . . . . . Assay Conditions . . . . . . . . . . . . . . . . . . .
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Requirement for Phosphoenolpyruvate Carboxylase in a Cyanobacterium

1990
Although 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
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Modification of maize phosphoenolpyruvate carboxylase by tetranitromethane

Phytochemistry, 1992
Abstract 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
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The regulation of phosphoenolpyruvate carboxylase in CAM plants

Trends in Plant Science, 2000
Phosphoenolpyruvate 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 ...
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Involvement of Ubiquitin in Phosphoenolpyruvate Carboxylase Degradation

Botanica Acta, 1993
AbstractWestern 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, Torsten Klockenbring, Carola Hunte, Margot Schulz   +3 more
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Phosphoenolpyruvate carboxylase from Acetobacter aceti

Archives of Microbiology, 1979
In 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
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In vivo phosphorylation of sorghum leaf phosphoenolpyruvate carboxylase

Biochimie, 1988
The 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, Jean Vidal, Pierre Le Maréchal, Pierre Gadal, Martine Thomas, Marie-Thérèse Guidici-Orticoni   +5 more
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The mechanism of inhibition of phosphoenolpyruvate carboxylase by quinolinic acid

Biochimica et Biophysica Acta (BBA) - Enzymology, 1972
Abstract 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, Buris R. Boshell, W.J. Reddy   +2 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 remarkable diversity of plant PEPC (phosphoenolpyruvate carboxylase): recent insights into the physiological functions and post-translational controls of non-photosynthetic PEPCs.

Biochemical Journal, 2011
PEPC [PEP (phosphoenolpyruvate) carboxylase] is a tightly controlled enzyme located at the core of plant C-metabolism that catalyses the irreversible β-carboxylation of PEP to form oxaloacetate and Pi.
B. O’Leary, Joonho Park, W. Plaxton
semanticscholar   +1 more source