This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate.
This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate.
not inhibited by phosphatidic acid, phosphatidylinositol, phosphatidylinositol 4-phosphate, lyso-phosphatidic acid, phosphatidylserine, phosphatidylcholine, and phosphatidylethanolamine
Atppc2 transcripts are found in all Arabidopsis organs suggesting that it is a housekeeping gene. Salt and drought exert a differential induction of PEPC gene expression in roots
Atppc2 transcripts are found in all Arabidopsis organs suggesting that it is a housekeeping gene. Salt and drought exert a differential induction of PEPC gene expression in roots
Atppc2 transcripts are found in all Arabidopsis organs suggesting that it is a housekeeping gene. Salt and drought exert a differential induction of PEPC gene expression in roots
Atppc2 transcripts are found in all Arabidopsis organs suggesting that it is a housekeeping gene. Salt and drought exert a differential induction of PEPC gene expression in roots
a double mutant lacking both isoforms Ppc1/Ppc2 exhibits a severe growth-arrest phenotype. The Ppc1/Ppc2 mutant accumulates more starch and sucrose than wild-type plants when seedlings are grown under normal conditions. Decreased PEPC activity in the mutant greatly reduces the synthesis of malate and citrate and severely suppresses ammonium assimilation. Nitrate levels in the double mutant are significantly lower than those in wild-type plants due to the suppression of ammonium assimilation. Starch and sucrose accumulation can be prevented and nitrate levels can be maintained by supplying the Ppc1/Ppc2 mutant with exogenous malate and glutamate
PEPC is involved in atmospheric CO2 fixation, C/N interaction and anaplerotic C-flux, energy supply for symbiotic bacteria, carbon storage in cell vacuoles, root malate/citrate excretion for abiotic stress acclimation, seed germination, seed development, and cell expansion
a double mutant lacking both isoforms Ppc1/Ppc2 exhibits a severe growth-arrest phenotype. The Ppc1/Ppc2 mutant accumulates more starch and sucrose than wild-type plants when seedlings are grown under normal conditions. Decreased PEPC activity in the mutant greatly reduces the synthesis of malate and citrate and severely suppresses ammonium assimilation. Nitrate levels in the double mutant are significantly lower than those in wild-type plants due to the suppression of ammonium assimilation. Starch and sucrose accumulation can be prevented and nitrate levels can be maintained by supplying the Ppc1/Ppc2 mutant with exogenous malate and glutamate
purified PPC1 is phosphorylated at Ser-11, in vivo phosphorylation of isoform PPC1 during phosphate stress also activates this enzyme at pH 7.3 by significantly lowering its Km(phosphoenolpyruvate) value and sensitivity to inhibition by L-malate and L-Asp, while increasing its activation by D-glucose-6-phosphate
Arabidopsis phosphoenolpyruvate carboxylase genes encode immunologically unrelated polypeptides and are differentially expressed in response to drought and salt stress
Meimoun, P.; Gousset-Dupont, A.; Lebouteiller, B.; Ambard-Bretteville, F.; Besin, E.; Lelarge, C.; Mauve, C.; Hodges, M.; Vidal, J.
The impact of PEPC phosphorylation on growth and development of Arabidopsis thaliana: molecular and physiological characterization of PEPC kinase mutants
The remarkable diversity of plant PEPC (phosphoenolpyruvate carboxylase): recent insights into the physiological functions and post-translational controls of non-photosynthetic PEPCs