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additional information
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modulation of phosphoenolpyruvate carboxylase in vivo by Ca2+, possible involvement of Ca2+ in up-regulation of PEPC-protein kinase
acylation
acetylation of PEPC at lysine 653 decreases enzymatic activity, leading to reduced glutamate production. NCgl0616, a sirtuin-type deacetylase, deacetylates K653-acetylated PEPC in vitro
acylation
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acetylation of PEPC at lysine 653 decreases enzymatic activity, leading to reduced glutamate production. NCgl0616, a sirtuin-type deacetylase, deacetylates K653-acetylated PEPC in vitro
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phosphoprotein
Amaranthus edulis
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PEPC proteins are phosphorylated in dry seeds, and PEPC phosphorylation does not occur in vivo during seed imbibition in the presence of 32P-phosphate
phosphoprotein
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a marked diurnal rhythm can be seen in the PEPC protein levels and phosphorylation status during May (summer month). In contrast, only the phosphorylation status increases during the day in December (winter month)
phosphoprotein
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PEPC is phosphorylated only during the dark period, especially at midnight
phosphoprotein
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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
phosphoprotein
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the phosphoenolpyruvate carboxylase kinase gene product PPCk1 is responsible for leaf PEPC phosphorylation
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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the enzyme may exist in a dephosphorylated form in cell grown in absence of phosphate and in cells grown in presence of phosphate
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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PEPC is phosphorylated only during the dark period, especially during the first 2 h of darkness
phosphoprotein
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PEPC is phosphorylated only during the dark period, especially during the first 2 h of darkness
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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in plants cultivated hydroponically at low phosphate levels, during the daytime the cluster root PEPC is activated by phosphorylation at its conserved N-terminal seryl residue. Darkness triggers a progressive reduction in PEPC phosphorylation to undetectable levels, and this is correlated with 75-80 % decreases in concentrations of sucrose and trehalose 6-phosphate
phosphoprotein
Lupinus albus var. Kiev
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in plants cultivated hydroponically at low phosphate levels, during the daytime the cluster root PEPC is activated by phosphorylation at its conserved N-terminal seryl residue. Darkness triggers a progressive reduction in PEPC phosphorylation to undetectable levels, and this is correlated with 75-80 % decreases in concentrations of sucrose and trehalose 6-phosphate
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phosphoprotein
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the protein phosphatase inhibitor, okadaic acid, promotes the phosphorylation of PEPCK
phosphoprotein
Musa cavendishii
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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Ser6 is phosphorylated. Ser6 phosphorylation of the p107 subunit increases KM-value of PEPC2 for phosphoenolpyruvate and sensitivity to L-malate, glutamic acid, and aspartic acid inhibition. Phosphorylation of subunit p107 is promoted during development of Ricinus communis but disappears during desiccation. The p107 stage VII becomes fully dephosphorylated in plants 48 h following excision of Ricinus communis pods or following 72 h of dark treatment of intact plants
phosphoprotein
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Ser6 is phosphorylated. Ser6 phosphorylation of the p107 subunit increases PEPC1 activity at pH 7.3 by decreasing its KM for phosphoenolpyruvate and sensitivity to L-malate inhibition, while enhancing glucose 6-phosphate activation
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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phosphorylation at Ser425 is promoted during seed development, Ser425 phosphorylation results in significant bacterial-type phosphoenolpyruvate carboxylase inhibition
phosphoprotein
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PTPC of castor oil seeds is activated by phosphorylation at Ser-11 during endosperm development
phosphoprotein
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phosphorylated at Ser451
phosphoprotein
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the enzyme is in vivo phosphorylated at Ser451
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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C4-PEPC is regulated by phosphorylation by a phosphoenolpyruvate carboxylase kinase, n-butanol leads to the partial inhibition of the C4-PEPC phosphorylation
phosphoprotein
monoubiquitinated isoform PPC2 is phosphorylated at its conserved N-terminal seryl phosphorylation site, i.e. Ser13
phosphoprotein
monoubiquitinated isoform PPC3 is phosphorylated at its conserved N-terminal seryl phosphorylation site, i.e. Ser7
phosphoprotein
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class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
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the guard cell enzyme is regulated by reversible phosphorylation of at least one isoform
ubiquitination
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PTPC of castor oil seeds is inhibited by monoubiquitination at Lys-628 during germination
ubiquitination
isoform PPC2 is monoubiquitinated in vivo, probybly at at the conserved residue Lys630
ubiquitination
isoform PPC3 is monoubiquitinated in vivo, probably at at the conserved residue Lys624
ubiquitination
isooform PPC4 is monoubiquitinated in vivo