Results 1 to 10 of about 2,068 (170)

Cell-cell heterogeneity in phosphoenolpyruvate carboxylase biases early cell fate priming in Dictyostelium discoideum. [PDF]

open access: yesFront Cell Dev Biol
Glucose metabolism is a key factor characterizing the cellular state during multicellular development. In metazoans, the metabolic state of undifferentiated cells correlates with growth/differentiation transition and cell fate determination. Notably, the
Abe K   +8 more
europepmc   +2 more sources

Genome-Wide Identification and Expression Analysis of the PEPC Gene Family in <i>Zanthoxylum armatum</i> Reveals Potential Roles in Environmental Adaptation. [PDF]

open access: yesBiology (Basel)
Phosphoenolpyruvate carboxylase (PEPC) is a crucial enzyme in plant photosynthesis and stress responses, yet its gene family remained uncharacterized in Zanthoxylum armatum.
Xu R   +12 more
europepmc   +2 more sources

Phosphoenolpyruvate carboxylase (PEPC) is essential for the glycolytic pathway and parasite proliferation in Babesia gibsoni

open access: yesAnimal Diseases
Apicomplexan parasites predominantly generate ATP and lactic acid through glycolysis and anaerobic glucose metabolism, incorporating CO2 into glycolysis via a stage-dependent phosphoenolpyruvate carboxylase (PEPC) mechanism.
Dong-Fang Li   +9 more
doaj   +2 more sources

Conservation and Divergence of PEPC Gene Family in Different Ploidy Bamboos. [PDF]

open access: yesPlants (Basel)
Phosphoenolpyruvate carboxylase (PEPC), as a necessary enzyme for higher plants to participate in photosynthesis, plays a key role in photosynthetic carbon metabolism and the stress response.
Cheng W   +5 more
europepmc   +2 more sources

Biochemical relationship of phosphoenolpyruvate carboxylases (PEPCs) from thermophilic archaea [PDF]

open access: yesFEMS Microbiology Letters, 1997
An archaeal phosphoenolpyruvate carboxylase (PEPC) was purified from an acidophilic extreme thermophile, Sulfolobus acidocaldarius. The native enzyme was a homotetramer of 260±20 kDa molecular mass composed of 60±5 kDa subunits. The enzyme appeared to have a temperature optimum of 90°C and a pH optimum of 8.0. The activity of S.
Yoshihiko Sako   +3 more
openaire   +2 more sources

Convergent molecular evolution of phosphoenolpyruvate carboxylase gene family in C4 and crassulacean acid metabolism plants [PDF]

open access: yesPeerJ, 2022
Phosphoenolpyruvate carboxylase (PEPC), as the key enzyme in initial carbon fixation of C4and crassulacean acid mechanism (CAM) pathways, was thought to undergo convergent adaptive changes resulting in the convergent evolution of C4 and CAM ...
Jiang-Ping Shu   +2 more
doaj   +2 more sources

An in vitro Coupled Assay for PEPC with Control of Bicarbonate Concentration

open access: yesBio-Protocol, 2021
Phosphoenolpyruvate carboxylase (PEPC) catalyzes a critical step in carbon metabolism in plants and bacteria, the irreversible reaction between bicarbonate and phosphoenolpyruvate to produce the C4 compound oxaloacetate.
Nicholas Moody   +2 more
doaj   +1 more source

Differential Expression, Tissue-Specific Distribution, and Posttranslational Controls of Phosphoenolpyruvate Carboxylase

open access: yesPlants, 2021
Phosphoenolpyruvate carboxylase (PEPC) is a ubiquitous cytosolic enzyme, which is crucial for plant carbon metabolism. PEPC participates in photosynthesis by catalyzing the initial fixation of atmospheric CO2 and is abundant in both C4 and crassulacean ...
Lorrenne Caburatan, Joonho Park
doaj   +1 more source

Screening of highly efficient photosynthetic hybrids of Oryza officinalis and analysis of their photosynthetic pathway genes

open access: yesPhotosynthetica, 2021
Hereditary properties of strong growth and huge accumulation of biomass in Oryza officinalis exhibit a great potential; however, the genes that code for its high photosynthesis performance are not established.
E.X. LI   +7 more
doaj   +1 more source

Light Regulation of the Photosynthetic Phospho enol pyruvate Carboxylase (PEPC) in Hydrilla verticillata [PDF]

open access: yesPlant and Cell Physiology, 2006
The submersed monocot, Hydrilla verticillata (L.f.) Royle, is a facultative C(4) NADP-malic enzyme (NADP-ME) plant in which the C(4) and Calvin cycles co-exist in the same cell. Futile cycling is avoided by an intracellular separation of carboxylases between the cytosol and chloroplasts. Of the two sequenced H.
Srinath, Rao   +2 more
openaire   +2 more sources

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