نتایج جستجو برای: pepc

تعداد نتایج: 297  

Journal: :Biological research 2007
Louis Leitao Jean-José Maoret Jean-Philippe Biolley

We quantified the ozone impact on levels of Zea mays L. cv. Chambord mRNAs encoding C4-phosphoenolpyruvate carboxylase (C4-PEPc), ribulose-l,5-bisphosphate carboxylase/oxygenase small and large subunits (Rubisco-SSU and Rubisco-LSU, respectively) and Rubisco activase (RCA) using real-time RT-PCR. Foliar pigment content, PEPc and Rubisco protein amounts were simultaneously determined. Two experi...

Journal: :The Plant journal : for cell and molecular biology 1997
M S Pathirana D A Samac R Roeven H Yoshioka C P Vance J S Gantt

Phosphoenolpyruvate carboxylase (PEPC) plays a crucial role in the assimilation of CO2 during symbiotic N2 fixation in legume root nodules. In this study, an alfalfa PEPC gene (PEPC-7), whose transcripts are found at elevated levels in nodules relative to either leaves or roots, has been isolated and characterized. The intron/exon structure of this gene is identical to that of most other plant ...

Journal: :Circulation 1974
J S Alpert F D Rickman J P Howe L Dexter J E Dalen

Systolic time intervals (STI) were measured in matched patients with and without right ventricular failure (RVF). STI were calculated from brachial arterial pressure tracings obtained at cardiac catheterization in four groups of patients: 1) controls, without RVF; 2) acute pulmonary embolism with and without acute RVF; 3) mitral stenosis, with and without chronic RVF; 4) primary pulmonary hyper...

2014
Janet Storm Sonal Sethia Gavin J. Blackburn Achuthanunni Chokkathukalam David G. Watson Rainer Breitling Graham H. Coombs Sylke Müller

Phospoenolpyruvate carboxylase (PEPC) is absent from humans but encoded in the Plasmodium falciparum genome, suggesting that PEPC has a parasite-specific function. To investigate its importance in P. falciparum, we generated a pepc null mutant (D10(Δpepc) ), which was only achievable when malate, a reduction product of oxaloacetate, was added to the growth medium. D10(Δpepc) had a severe growth...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2010
Chisato Masumoto Shin-Ichi Miyazawa Hiroshi Ohkawa Takuya Fukuda Yojiro Taniguchi Seiji Murayama Miyako Kusano Kazuki Saito Hiroshi Fukayama Mitsue Miyao

Phosphoenolpyruvate carboxylase (PEPC) is a key enzyme of primary metabolism in bacteria, algae, and vascular plants, and is believed to be cytosolic. Here we show that rice (Oryza sativa L.) has a plant-type PEPC, Osppc4, that is targeted to the chloroplast. Osppc4 was expressed in all organs tested and showed high expression in the leaves. Its expression in the leaves was confined to mesophyl...

2010
José Antonio Monreal Francisco Javier López-Baena Jean Vidal Cristina Echevarría Sofía García-Mauriño

The photosynthetic phosphoenolpyruvate carboxylase (C(4)-PEPC) is regulated by phosphorylation by a phosphoenolpyruvate carboxylase kinase (PEPC-k). In Digitaria sanguinalis mesophyll protoplasts, this light-mediated transduction cascade principally requires a phosphoinositide-specific phospholipase C (PI-PLC) and a Ca(2+)-dependent step. The present study investigates the cascade components at...

Journal: :Journal of experimental botany 2003
Kentaro Toyota Nozomu Koizumi Fumihiko Sato

Phosphoenolpyruvate carboxylase (PEPC), which catalyses the carboxylation of phosphoenolpyruvate using HCO(3)(-) to generate oxaloacetic acid, is an important enzyme in the primary metabolism of plants. Although the PEPC genes (ppc) comprise only a small gene family, the function of each gene is not clear, except for roles in C(4) photosynthesis and CAM. Three PEPC genes (Nsppc1-3) from the C(3...

Journal: :The Journal of biological chemistry 2009
Annika Schmid Wibke Neumayer Konrad Trülzsch Lars Israel Axel Imhof Manfred Roessle Guido Sauer Susanna Richter Susan Lauw Eva Eylert Wolfgang Eisenreich Jürgen Heesemann Gottfried Wilharm

Pathogenic yersiniae utilize a type three secretion system (T3SS) to inject Yop proteins into host cells in order to undermine their immune response. YscM1 and YscM2 proteins have been reported to be functionally equivalent regulators of the T3SS in Yersinia enterocolitica. Here, we show by affinity purification, native gel electrophoresis and small angle x-ray scattering that both YscM1 and Ys...

Journal: :Journal of Experimental Botany 2002

Journal: :Plant physiology 2003
Rosario Alvarez Sofía García-Mauriño Ana-Belén Feria Jean Vidal Cristina Echevarría

Higher plant phosphoenolpyruvate carboxylase (PEPC) is subject to in vivo phosphorylation of a regulatory serine located in the N-terminal domain of the protein. Studies using synthetic peptide substrates and mutated phosphorylation domain photosynthetic PEPC (C4 PEPC) suggested that the interaction of phosphoenolpyruvate carboxylase kinase (PEPCk) with its target was not restricted to this dom...

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