Results 11 to 20 of about 21,076 (117)

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

open access: yesAnimal Diseases
AbstractApicomplexan 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. Although the role of PEPC in plant and bacterial carbon fixation is well documented, its function within Babesia remains ...
Dong-Fang Li   +9 more
openaire   +3 more sources

Identification and expression analysis of phosphoenolpyruvate carboxylase (PEPC) and PEPC kinase genes in C3 plants [PDF]

open access: yes, 2004
Phosphoenolpyruvate carboxylase (PEPc) is a cytosolic enzyme that plays a wide range of roles in different tissues of higher plants. A photosynthetic isoform of PEPc catalyses the primary fixation of CO2 in C4 and CAM plants.
Sullivan, Jonathan Stuart
core   +7 more sources

Phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxylase kinase isoenzymes play an important role in the filling and quality of Arabidopsis thaliana seed [PDF]

open access: yes, 2022
Three plant-type phosphoenolpyruvate carboxylase (PPC1 to PPC3) and two phosphoenolpyruvate carboxylase kinase (PPCKs: PPCK1 and 2) genes are present in the Arabidopsis thaliana genome. In seeds, all PPC genes were found to be expressed.
Feria Bourrellier, Ana Belén   +16 more
core   +1 more source

Oligomerization and characteristics of phosphoenolpyruvate carboxylase in Synechococcus PCC 7002

open access: yes, 2020
Phosphoenolpyruvate carboxylase (PEPc) is an essential enzyme in plants. A photosynthetic form is present both as dimer and tetramer in C4 and CAM metabolism. Additionally, non-photosynthetic PEPcs are also present. The single, non-photosynthetic PEPc of
Durall de la Fuente, Claudia,   +7 more
core   +1 more source

A Ca2+-dependent protein kinase phosphorylates phosphoenolpyruvate carboxylase in maize [PDF]

open access: yes, 1992
In C4 plants the activity of phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) is regulated by phosphorylation/dephosphorylation which is mediated by light/dark signals.
Ogawa, Noriyuki   +5 more
core   +1 more source

Phosphorylation of C4 And Non-C4 Phosphoenolpyruvate Carboxylase from Panicum and the Kinetic Behaviour of Phosphorylated and Non-Phosphorylated PEPC [PDF]

open access: yes, 2019
The C4 photosynthesis pathway is more efficient than C3 photosynthesis due to the capability of phosphoenolpyruvate carboxylase (PEPC) that provides a CO2 high concentration at Rubisco, thus reducing the photorespiration rate.
Zawawi, Dhiya Dalila
core   +5 more sources

PEPC gene family data

open access: yes, 2021
PEPC gene family identified from 17 genomic datasets in “Convergent molecular evolution of phosphoenolpyruvate carboxylase gene family in C4 and crassulacean acid metabolism ...
Jiang-Ping Shu (11656264)
core   +1 more source

Expression Profiles of Phosphoenolpyruvate Carboxylase and Phosphoenolpyruvate Carboxylase Kinase Genes in Phalaenopsis, Implications for Regulating the Performance of Crassulacean Acid Metabolism [PDF]

open access: yes, 2018
Phalaenopsis is one of the most important potted plants in the ornamental market of the world. Previous reports implied that crassulacean acid metabolism (CAM) orchids at their young seedling stages might perform C3 or weak CAM photosynthetic pathways ...
Teen-Chi Cheng   +6 more
core   +1 more source

Phosphoenolpyruvate carboxylase (PEPC) in extracts of neisseria gonorrhoeae. [PDF]

open access: yes, 1975
The enzymatic carboxylation of phosphoenolpyruvate by cell free extracts of Neisseria gonorrhoeae was examined and determined to be similar to the reaction catalysed by phosphoenolpyruvate carboxylase (PEPC).
Cox, David L.
core  

Phosphoenolpyruvate carboxylase from C4 leaves is selectively targeted for inhibition by anionic phospholipids

open access: yes, 2010
Phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) is an enzyme playing a crucial role in photosynthesis of C4 plants. Here, we identify anionic phospholipids as novel regulators that inhibit C4 PEPC activity and provide evidence that the enzyme ...
Echevarría, Cristina   +9 more
core   +1 more source

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