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ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
-
-
-
?
phosphate + oxaloacetate
H2O + phosphoenolpyruvate + CO2
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
Phosphoenolpyruvate + CO2
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
additional information
?
-
phosphate + oxaloacetate
H2O + phosphoenolpyruvate + CO2
-
-
-
-
?
phosphate + oxaloacetate
H2O + phosphoenolpyruvate + CO2
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
Phosphoenolpyruvate + CO2
?
-
key enzyme mediating the primary carbon assimilation
-
-
?
Phosphoenolpyruvate + CO2
?
-
key enzyme in the supply of carbon skeleton for the assimilation of nitrogen by green algae
-
-
?
Phosphoenolpyruvate + CO2
?
-
key enzyme in the supply of carbon skeleton for the assimilation of nitrogen by green algae
-
-
?
Phosphoenolpyruvate + CO2
?
-
in C4 plants the enzyme catalyzes the first step of the C4 dicarboxylic acid pathway. In CAM plants the enzyme functions in CO2 fixation
-
-
?
Phosphoenolpyruvate + CO2
?
-
possible role of the enzyme in controlling a circadian rhythm of CO2 fixation
-
-
?
Phosphoenolpyruvate + CO2
?
-
the enzyme is involved in autotrophic CO2 fixation
-
-
?
Phosphoenolpyruvate + CO2
?
Molinema dessetae
-
enzyme at the branchpoint of glycolysis and Krebs cycle
-
-
?
Phosphoenolpyruvate + CO2
?
-
function is probably anaplerotic
-
-
?
Phosphoenolpyruvate + CO2
?
-
Umbilicus rupestris switches from C3 photosynthesis to an incomplete form of crassulacean acid metabolism, referred to as CAM-idling, when exposed to water stress. This switch is accompanied by an increase in the activity of phosphoenolpyruvate carboxylase
-
-
?
Phosphoenolpyruvate + CO2
?
-
three PEPC isoforms: one is the C4-form PEPC, which plays a cardinal role in the initial CO2-fixation of C4 photosynthesis by capturing atmospheric CO2 into C4-dicarboxylic acids, the second one is a C3-housekeeping PEPC, which plays anaplerotic roles by replenishing C4-dicarboxylic acids in the citric acid cycle for synthesis of cell constituents, the root-form PEPC plays various anaplerotic roles, including providing the carbon skeletons for nitrogen assimilation, pH maintenance, and osmolarity regulation
-
-
?
Phosphoenolpyruvate + CO2
?
-
key enzyme in CO2 assimilation pathway of C4 and CAM plants
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
Amaranthus edulis
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
Coccochloris peniocystis
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
Crassula argentea
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
Crassula argentea
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
Molinema dessetae
-
enzyme does not catalyze the reverse reaction
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
the organism expresses, regulates and assembles divergent PEPC polypeptides. This probably serves an adaptive pupose by posing these organism for survival in different environments varying in nutrient content
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
Panicum schenckii
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
moderated water stress applied to Pinus halepensis has no effect on PEPC activity. Ozone stress induces a dramatic increase of PEPC activity in pine needles
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
by shifting to CAM in the C4 Portulaca a nes PEPC isoform may be synthesized to meet CAM requirements
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
the enzyme is responsible for primary CO2 fixation. PEPC activity and regulationm are modified upon drought stress treatment in a way that allows Portulaca oleracea to perform a CAM-like metabolism
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
Sorghum sp.
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
Thermostichus vulcanus
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
NaCl and LiCl induce enzyme expression in roots. Other abiotic stresses affecting water status, such as drought or cold, induce PEPC expression. Important role of the enzyme in the adaption of plants to environmental changes
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
key enzyme in fixation of atmospheric CO2 in C4 and crassulacean acid metabolism
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
concerted sequential allosteric mechanism
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract of the C4 plant
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract of the C3 plant
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
Amaranthus edulis
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
it is suggested that Ca2+ regulates PEPC, at an upstream level, such as transcription, by modulating PEPC-protein kinase, thus facilitating the light activation of PEPC
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
Coccochloris peniocystis
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
PEPC plays a role in respiratory carbon dioxide refixation while generating malate to support amino acid and/or fatty acids biosynthesis
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
Molinema dessetae
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?, ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
Musa cavendishii
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
WP_019935846
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
r
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
r
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
r
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
Thermosynechococcus vestitus
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
additional information
?
-
recombinant PPC4 forms class-2 PEPC when combined with class-1 PEPCs
-
-
?
additional information
?
-
-
BTPC tightly interacts with co-expressed PTPC to form the allosterically-desensitized class-2 PEPC heteromeric complex
-
-
?
additional information
?
-
PEPC may be involved in protein biosynthesis during grain development, and it may have an important role in regulating carbon and nitrogen metabolism in the ear organ of wheat
-
-
?
additional information
?
-
-
the guard cell enzyme is regulated by reversible phosphorylation of at least one isoform
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + phosphoenolpyruvate + CO2
ATP + oxaloacetate
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
Phosphoenolpyruvate + CO2
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
additional information
?
-
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + HCO3-
-
-
-
-
?
Phosphoenolpyruvate + CO2
?
-
key enzyme mediating the primary carbon assimilation
-
-
?
Phosphoenolpyruvate + CO2
?
-
key enzyme in the supply of carbon skeleton for the assimilation of nitrogen by green algae
-
-
?
Phosphoenolpyruvate + CO2
?
-
key enzyme in the supply of carbon skeleton for the assimilation of nitrogen by green algae
-
-
?
Phosphoenolpyruvate + CO2
?
-
in C4 plants the enzyme catalyzes the first step of the C4 dicarboxylic acid pathway. In CAM plants the enzyme functions in CO2 fixation
-
-
?
Phosphoenolpyruvate + CO2
?
-
possible role of the enzyme in controlling a circadian rhythm of CO2 fixation
-
-
?
Phosphoenolpyruvate + CO2
?
-
the enzyme is involved in autotrophic CO2 fixation
-
-
?
Phosphoenolpyruvate + CO2
?
Molinema dessetae
-
enzyme at the branchpoint of glycolysis and Krebs cycle
-
-
?
Phosphoenolpyruvate + CO2
?
-
function is probably anaplerotic
-
-
?
Phosphoenolpyruvate + CO2
?
-
Umbilicus rupestris switches from C3 photosynthesis to an incomplete form of crassulacean acid metabolism, referred to as CAM-idling, when exposed to water stress. This switch is accompanied by an increase in the activity of phosphoenolpyruvate carboxylase
-
-
?
Phosphoenolpyruvate + CO2
?
-
three PEPC isoforms: one is the C4-form PEPC, which plays a cardinal role in the initial CO2-fixation of C4 photosynthesis by capturing atmospheric CO2 into C4-dicarboxylic acids, the second one is a C3-housekeeping PEPC, which plays anaplerotic roles by replenishing C4-dicarboxylic acids in the citric acid cycle for synthesis of cell constituents, the root-form PEPC plays various anaplerotic roles, including providing the carbon skeletons for nitrogen assimilation, pH maintenance, and osmolarity regulation
-
-
?
Phosphoenolpyruvate + CO2
?
-
key enzyme in CO2 assimilation pathway of C4 and CAM plants
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
the organism expresses, regulates and assembles divergent PEPC polypeptides. This probably serves an adaptive pupose by posing these organism for survival in different environments varying in nutrient content
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
moderated water stress applied to Pinus halepensis has no effect on PEPC activity. Ozone stress induces a dramatic increase of PEPC activity in pine needles
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
by shifting to CAM in the C4 Portulaca a nes PEPC isoform may be synthesized to meet CAM requirements
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
the enzyme is responsible for primary CO2 fixation. PEPC activity and regulationm are modified upon drought stress treatment in a way that allows Portulaca oleracea to perform a CAM-like metabolism
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
NaCl and LiCl induce enzyme expression in roots. Other abiotic stresses affecting water status, such as drought or cold, induce PEPC expression. Important role of the enzyme in the adaption of plants to environmental changes
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
-
key enzyme in fixation of atmospheric CO2 in C4 and crassulacean acid metabolism
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract of the C4 plant
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract of the C3 plant
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
it is suggested that Ca2+ regulates PEPC, at an upstream level, such as transcription, by modulating PEPC-protein kinase, thus facilitating the light activation of PEPC
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
PEPC plays a role in respiratory carbon dioxide refixation while generating malate to support amino acid and/or fatty acids biosynthesis
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
-
-
-
-
?
additional information
?
-
recombinant PPC4 forms class-2 PEPC when combined with class-1 PEPCs
-
-
?
additional information
?
-
PEPC may be involved in protein biosynthesis during grain development, and it may have an important role in regulating carbon and nitrogen metabolism in the ear organ of wheat
-
-
?
additional information
?
-
-
the guard cell enzyme is regulated by reversible phosphorylation of at least one isoform
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
WP_019935846
32% of the activity with Mg2+
Cd2+
-
28% of the activation with Mg2+
Cu2+
WP_019935846
73% of the activity with Mg2+
Fe2+
-
12% of the activation with Mg2+
K+
-
12 mM, stimulates by 40%
NaCl
Coccochloris peniocystis
-
activation between 25 and 200 mM to a maximum of 14% a at 75 mM
Zn2+
Coccochloris peniocystis
-
60% of the activation with Mg2+
Co2+
-
divalent cation required, Mn2+, Co2+ and Mg2+. Co2+ is less effective than Mg2+ or Mn2+
Co2+
-
maximal activity at 1 mM Co2+, strong decrease of activity above 4 mM
Co2+
PepcA catalyzes formation of oxaloacetate in the presence of Mg2+, Mn2+, or Co2+ but not in the absence of a divalent metal ion
Co2+
Coccochloris peniocystis
-
60% of the activation with Mg2+
Co2+
-
divalent cation required, Mn2+, Co2+ and Mg2+. Co2+ is less effective than Mg2+ or Mn2+
Co2+
-
18% of the activation with Mg2+
Co2+
-
30% of the activation with Mg2+
Mg2+
-
Km: 0.77 mM
Mg2+
-
divalent cation required, Mn2+, Co2+ and Mg2+
Mg2+
Amaranthus edulis
-
-
Mg2+
-
desensitization by bicarbonate
Mg2+
-
absolute dependence
Mg2+
-
absolute dependence for a divalent cation, Km: 0.084 mM
Mg2+
-
absolute requirement for divalent cation is satisfied by Mg2+
Mg2+
required for activity, PepcA catalyzes formation of oxaloacetate in the presence of Mg2+, Mn2+, or Co2+ but not in the absence of a divalent metal ion
Mg2+
Coccochloris peniocystis
-
activates
Mg2+
Coccochloris peniocystis
-
Km: 0.27 mM
Mg2+
-
KM-value for the enzyme from roots grown in presence of Fe2+ is 0.93 mM, The KM-value from enzyme grown in absence of Fe2+ is 0.91 mM
Mg2+
-
divalent cation required, Mn2+, Co2+ and Mg2+
Mg2+
-
divalent cation required, Mg2+ is the best activator
Mg2+
Molinema dessetae
-
Mg2+ or Mn2+ required
Mg2+
-
p102 phosphorylation is absolutely dependent upon the presence of MgCl2
Mg2+
WP_019935846
best activator
Mg2+
-
Mg2+ or Mn2+ required
Mg2+
absolutely dependent on, PPC4 exhibits a 4fold higher specific activity with saturating (10mM) Mg2+ relative to Mn2+
Mg2+
the enzyme activity is completely dependent on the presence of Mg2+. The enzyme activity could not be reconstituted by the addition of Mn2+ instead of Mg2+
Mg2+
-
divalent cation required, Mg2+ is the best activator
Mg2+
-
the enzyme absolutely requires Mg2+ and cannot utilize Mn2+ instead, maximal activity at 1 mM, decrease of activity at higher concentrations
Mg2+
-
half-maximal activity at 0.1 mM
Mg2+
-
Km for isoenzyme PC-II: 0.015 mM
Mg2+
-
Km for isoenzyme PC-I: 0.032 mM
Mn2+
-
divalent cation required, Mn2+, Co2+ and Mg2+
Mn2+
-
maximal activity at 0.5 mM Mn2+, strong decrease of activity above 2 mM
Mn2+
-
absolute dependence
Mn2+
PepcA catalyzes formation of oxaloacetate in the presence of Mg2+, Mn2+, or Co2+ but not in the absence of a divalent metal ion
Mn2+
Coccochloris peniocystis
-
80% of the activation with Mg2+
Mn2+
-
23% of the activation with Mg2+
Mn2+
Molinema dessetae
-
Mg2+ or Mn2+ required
Mn2+
-
Mg2+ or Mn2+ required
Mn2+
-
68% of the activation with Mg2+. At suboptimal concentrations of phosphoenolpyruvate and HCO3-, Mn2+ is more effective than Mg2+
Mn2+
-
Km for isoenzyme PC-II: 0.0067 mM
Mn2+
-
Km for isoenzyme PC-I: 0.0102 mM
phosphate
-
activates
phosphate
-
activates at pH 7 in absence of glycerol, inhibits under other assay conditions
phosphate
-
the night form of the enzyme is phosphorylated, the phosphate is covalently bound to Ser, the day form of the enzyme is dephosphorylated
phosphate
-
the enzyme from root is phosphorylated by both mammalian cAMP-dependent protein kinase and maize leaf protein kinase, the phosphorylated enzyme is less sensitive to malate
additional information
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract
additional information
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2+ toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2+ toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
Musa cavendishii
-
Cd2+ toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2+ toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
WP_019935846
2.8% activity in absence of divalent cation
additional information
-
2.8% activity in absence of divalent cation
additional information
-
Cd2+ toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3-bromophenyl)-4-(3-hydroxybenzylidene)-pyrazolidine-3,5-dione
2-(4-methoxyphenyl)-3-phenyl-quinoxaline
-
3,3-dichloro-2-(dihydroxyphosphinoylmethyl) propenoate
-
micromolar inhibitor
alpha-Hydroxy-2-pyridylmethanesulfonate
Coccochloris peniocystis
-
-
alpha-ketoglutarate
Thermostichus vulcanus
10 mM, 9% inhibition
Butanoate
decreases PEPC activity and restricts the stimulation by abscisic acid
D-fructose
Thermostichus vulcanus
10 mM, 19% inhibition
D-fructose 1,6-bisphosphate
-
D-Fructose 1-phosphate
Thermostichus vulcanus
10 mM, 26% inhibition
D-fructose 2,6-diphosphate
Thermostichus vulcanus
0.3 mM, 35% inhibition
D-fructose 6-phosphate
99% residual activity at 2 mM
D-glucose 1-phosphate
95% residual activity at 2 mM
D-glucose 6-phosphate
93% residual activity at 2 mM
diethyl dicarbonate
-
causes dissociation of the enzyme into dimers and monomers
fructose 1,6-diphosphate
-
-
glutamate
-
IC50 of phospho-PEPC1: 2.1 mM, IC50 of dephospho-PEPC1: 2.2 mM; IC50 of phospho-PEPC2: 4.1 mM, IC50 of dephospho-PEPC2: 7.0 mM, enzyme form PEPC2
glycerol 3-phosphate
98% residual activity at 2 mM
guanidine hydrochloride
-
-
Hg2+
-
5 mM, in presence of 5 mM Mg2+
isocitrate
Coccochloris peniocystis
-
-
KCl
-
0.05-1.0 M, 60% inhibition at 0.25 M, 27% inhibition at 0.1 M
L-glutamate
very low sensitivities to allosteric inhibitors aspartate and glutamate; very low sensitivities to allosteric inhibitors aspartate and glutamate
Mg-(1,2-epoxypropylphosphonic acid) complex
-
-
Mg2+
-
free, non-competitive. Substrate inhibition by Mg-phosphoenolpyruvate is caused by inhibition by high Mg2+ and ionic strength
p-hydroxymercuribenzoate
-
glutathione protects
phosphatidylinositol 4-phosphate
phosphoenolpyruvate
-
above 1 mM
Picolinic acid
Coccochloris peniocystis
-
-
quinolinic acid
Coccochloris peniocystis
-
-
SO42-
Coccochloris peniocystis
-
-
(+)-catechin
-
(3-bromophenyl)-4-(3-hydroxybenzylidene)-pyrazolidine-3,5-dione
compound has a selectivity factor of 16.6 for C4 plant PepC over C3 plant PepC
(3-bromophenyl)-4-(3-hydroxybenzylidene)-pyrazolidine-3,5-dione
compound has a selectivity factor of 16.6 over C3 PepC
2-oxoglutarate
-
-
2-oxoglutarate
Coccochloris peniocystis
-
-
2-oxoglutarate
-
potent inhibitor at pH 7 in absence of glycerol, but its effectiveness is decreased by raising the pH to 8 and/or by adding glycerol
2-oxoglutarate
-
inhibition of enzyme form PEPC I and PEPC II, no inhibition of enzyme form PEPC III
2-oxoglutarate
-
isoenzyme PEPC1 is more sensitive to inhibition than isoenzyme PEPC2
ADP
-
10mM, 57% inhibition in presence of 5 mM Mg2+, 46% inhibition in presence of 15 mM Mg2+
AG 1433
i.e. 2-(3,4-dihydroxyphenyl)-6,7-dimethylquinoxaline
AG 1433
i.e. 2-(3,4-dihydroxyphenyl)-6,7-dimethylquinoxaline
AMP
-
slight
AMP
-
10mM, 16% inhibition in presence of 5 mM Mg2+, 12% inhibition in presence of 15 mM Mg2+
Asp
-
-
Asp
-
potent inhibitor at pH 7 in absence of glycerol, but its effectiveness is decreased by raising the pH to 8 and/or by adding glycerol
Asp
-
at pH 7.2, weak competitive inhibition for enzyme form PEPC I, strong competitive inhibition for enzyme form PEPC II and enzyme form PEPC III
Asp
-
isoenzyme PEPC1 is more sensitive to inhibition than isoenzyme PEPC2
aspartate
-
the enzyme loses about 95% activity when the aspartate concentration is more than 2 mM
aspartate
-
IC50 of phospho-PEPC1: 0.35 mM, IC50 of dephospho-PEPC1: 0.32 mM; IC50 of phospho-PEPC2: 2.6 mM, IC50 of dephospho-PEPC2: 4.5 mM, enzyme form PEPC2
ATP
-
-
ATP
Coccochloris peniocystis
-
-
ATP
-
10mM, 92% inhibition in presence of 5 mM Mg2+, 65% inhibition in presence of 15 mM Mg2+
ATP
-
2 mM, 65% decreases of activity of PEPC1 at pH 7.3, 13% decrease in activity of PEPC2 at pH 8
ATP
Thermostichus vulcanus
5.0 mM, 57% inhibition
Ca2+
-
5 mM, in presence of 5 mM Mg2+, 83% inhibition
Ca2+
-
substitution of 20 mM CaCl2 for 20 mM MgCl2 results in 90-100% inhibition
Cd2+
-
5 mM, in presence of 5 mM Mg2+
Cd2+
Molinema dessetae
-
-
citrate
-
-
citrate
-
strong inhibition
citrate
Coccochloris peniocystis
-
-
citrate
-
potent inhibitor at pH 7 in absence of glycerol, but its effectiveness is decreased by raising the pH to 8 and/or by adding glycerol
citrate
1 mM, 86% residual activity
Co2+
-
maximal activity at 1 mM Co2+, strong decrease of activity above 4 mM
Co2+
-
5 mM, in presence of 5 mM Mg2+
Cu2+
-
-
Cu2+
Molinema dessetae
-
-
epigallocatechin gallate
-
epigallocatechin gallate
-
Fe2+
-
-
Fe2+
Molinema dessetae
-
-
fumarate
-
-
fumarate
1 mM, 75% residual activity
fumarate
Thermostichus vulcanus
10 mM, 31% inhibition
Glu
-
-
Glu
-
potent inhibitor at pH 7 in absence of glycerol, but its effectiveness is decreased by raising the pH to 8 and/or by adding glycerol
Glu
-
inhibition of enzyme form PEPC I and PEPC II, no inhibition of enzyme form PEPC III
Glu
-
isoenzyme PEPC1 is more sensitive to inhibition than isoenzyme PEPC2
GTP
-
-
GTP
-
10mM, 58% inhibition in presence of 5 mM Mg2+, 15% inhibition in presence of 15 mM Mg2+
L-Asp
-
-
L-Asp
L-Asp competitively inhibits the enzyme with respect to the substrate, Mg2+-phosphoenolpyruvate
L-Asp
-
2 mM, 95% decreases of activity of PEPC1 at pH 7.3, 49% decrease in activity of PEPC2 at pH 8
L-Asp
Thermostichus vulcanus
more sensitive to inhibition by Asp at pH 9.0 than at pH 7.0
L-aspartate
-
-
L-aspartate
-
10 mM, 41% inhibition in presence of 5 mM Mg2+ or 15 mM Mg2+
L-aspartate
very low sensitivities to allosteric inhibitors aspartate and glutamate; very low sensitivities to allosteric inhibitors aspartate and glutamate
L-aspartate
98% residual activity at 2 mM
L-aspartate
allosteric inhibitor
L-aspartate
-
4 mM, complete inhibition
L-aspartate
1 mM, 85% residual activity for wild-type, 60% for mutant K954E, respectively
L-Glu
-
-
L-Glu
-
2 mM, 96% decreases of activity of PEPC1 at pH 7.3, 22% decrease in activity of PEPC2 at pH 8
L-malate
Amaranthus edulis
-
-
L-malate
sensitivity to L-malate is decreased after abscisic acid treatment
L-malate
-
IC50: 3.84 mM for enzyme from mesocarop, stored in air, 5.95 mM for enzyme from mesocarop stored in 20% CO2, 2.01 mM for enzyme from peel stored in air
L-malate
-
weak inhibition at physiological pH values
L-malate
1 mM, 30% residual activity, 80% for mutant K946E, respectively
L-malate
84% residual activity at 2 mM
L-malate
allosteric inhibitor
L-malate
-
the inhibition by 0.16 mM L-malate, pH 7.3, decreases from 70 to 30%, along with a consistent increase in IC50 from 0.075 mM to 0.22 mM after 5 days of germination
L-malate
-
10 mM, 48% inhibition
L-malate
1 mM, 77% residual activity, 60% for mutant K954E, respectively
L-malate
-
inhibits wild-type enzyme
lyso-phosphatidic acid
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 45% of the control activity
lyso-phosphatidic acid
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 45% of the control activity
malate
-
desensitization by bicarbonate
malate
-
dry heat, dark, 25°C: 96% inhibition, 45°C: 84% inhibition/dry heat, light, 25°C: 59% inhibition, 45°C: 31.2% inhibition/wet heat, dark, 25°C: 94%, 45°C: 76% inhibition /wet heat, light, 25°C: 46% inhibition, 45°C: 17% inhibition
malate
-
IC50: 8 mM for PEPC activity in situ, 1.5 mM for PEPC activity in vitro
malate
-
potent inhibitor at pH 7 in absence of glycerol, but its effectiveness is decreased by raising the pH to 8 and/or by adding glycerol
malate
-
the day form of the enzyme is 10times more sensitive than the night form of the enzyme
malate
-
competitive inhibitor of enzyme form PEPC I and enzyme form PEPC III, mixed-type inhibitor for enzyme form PEPC II
malate
Musa cavendishii
-
-
malate
-
2 mM, 96% decreases of activity of PEPC1 at pH 7.3, 59% decrease in activity of PEPC1 at pH 8
malate
-
IC50 of phospho-PEPC1: 0.075 mM, IC50 of dephospho-PEPC1: 0.029 mM; IC50 of phospho-PEPC2: 0.57 mM, IC50 of dephospho-PEPC2: 1.47 mM, enzyme form PEPC2
malate
-
competitive; L-malate
malate
-
feedback inhibitor
malate
-
reduction of the inhibitory effect by ethylene glycol and bicarbonate
malate
-
the phosphorylated enzyme is less sensitive to malate
Maleate
Coccochloris peniocystis
-
-
malonate
weak inhibitor
malonate
Coccochloris peniocystis
-
-
malonate
-
inhibits at pH 7.8, increases activity at pH 5.8
Mn2+
-
maximal activity at 0.5 mM Mn2+, strong decrease of activity above 2 mM
Mn2+
-
5 mM, in presence of 5 mM Mg2+, 72% inhibition
Mn2+
-
substitution of 20 mM MnCl2 for 20 mM MgCl2 results in 90-100% inhibition
NaCl
-
0.05-1.0 M, 60% inhibition at 0.25 M, 27% inhibition at 0.1 M
NaCl
-
200 mM, 50% inhibition
Ni2+
-
weak
oxaloacetate
-
-
oxaloacetate
Coccochloris peniocystis
-
-
PCMB
-
glutathione protects
PCMB
-
causes dissociation of the enzyme into dimers and monomers
phosphate
Coccochloris peniocystis
-
-
phosphate
-
activates at pH 7 in absence of glycerol, inhibits under other assay conditions
phosphate
-
orthophosphate is noncompetitive with phosphoenolpyruvate
phosphatidic acid
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 40% of the control activity. Inclusion of D-glucose 6-phosphate or L-malate do not change the effect of phosphatidic acid on PEPC, preincubation of the enzyme with 5 mM phosphoenolpyruvate prior to the addition of phosphatidic acid did not prevent inactivation either. The incubation of phosphatidic acid-inactivated PEPC with protein kinase A does not restore PEPC activity
phosphatidic acid
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 40% of the control activity. Inclusion of D-glucose 6-phosphate or L-malate do not change the effect of phosphatidic acid on PEPC, preincubation of the enzyme with 5 mM phosphoenolpyruvate prior to the addition of phosphatidic acid did not prevent inactivation either. The incubation of phosphatidic acid-inactivated PEPC with protein kinase A does not restore PEPC activity
phosphatidylinositol
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 40% of the control activity
phosphatidylinositol
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 40% of the control activity
phosphatidylinositol 4-phosphate
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 50% of the control activity
phosphatidylinositol 4-phosphate
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 50% of the control activity
phosphatidylserine
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 80% of the control activity
phosphatidylserine
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 80% of the control activity
pyruvate
-
-
pyruvate
-
inhibition of enzyme form PEPC I and PEPC II, no inhibition of enzyme form PEPC III
quercetin
-
-
rutin
-
-
succinate
-
-
Zn2+
-
5 mM, in presence of 5 mM Mg2+
Zn2+
-
substitution of 20 mM ZnCl2 for 20 mM MgCl2 results in 90-100% inhibition
Zn2+
Molinema dessetae
-
-
additional information
-
not inhibited by phosphatidic acid, phosphatidylinositol, phosphatidylinositol 4-phosphate, lyso-phosphatidic acid, phosphatidylserine, phosphatidylcholine, and phosphatidylethanolamine
-
additional information
-
the enzyme is poorly affected by L-Glu and L-Asp
-
additional information
not inhibited by 2-(4-methoxyphenyl)-3-phenyl-quinoxaline
-
additional information
-
phosphatidylcholine and phosphatidylethanolamine have no effect on enzyme activity
-
additional information
Thermostichus vulcanus
-
the enzyme is almost insensitive to feedback inhibition at neutral pH
-
additional information
-
phosphatidylcholine and phosphatidylethanolamine have no effect on enzyme activity
-
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1,2-Epoxypropylphosphonic acid
-
-
2-mercaptoethanol
-
activates
3-phosphoglycerate
Thermostichus vulcanus
slight stimulation
6-benzylaminopurine
-
natural cytokinin BAP
acetoacetyl-CoA
-
activates
alpha-glycerophosphate
-
activates
D-fructose 1,6-bisphosphate
-
D-Glucose-6-phosphate
activation of PEPC is enhanced after abscisic acid treatment
dihydroxyacetone phosphate
fructose 1,6-bisphosphate
fructose 1,6-diphosphate
Thermostichus vulcanus
activates
fructose diphosphate
-
activates
fusicoccin
-
rapid activation, reduces sensitivity towards the feedback-inhibitor malate
galactose 6-phosphate
-
activates at pH 7.8
Gln
Thermostichus vulcanus
slight stimulation
Glu
Thermostichus vulcanus
slight stimulation
heptanoyl-CoA
-
activates
malate
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
malonate
-
inhibits at pH 7.8, increases activity at pH 5.8
methylamine
increases the PEPC activity and enhances the effect of abscisic acid
N-isopropoxycarbonyl-4-chlorophenylcarbamoyl-ethanolamine
-
synthetic preparation exhibiting cytokinin activity: kartolin-4
O-isopropyl-N-2-hydroxyethylcarbamate
-
synthetic preparation exhibiting cytokinin activity: kartolin-2
phosphate
-
dry heat, dark, 25°C: 222% activation, 45°C: 275% activation/dry heat, light, 25°C: 321% activation, 45°C: 636% activation/wet heat, dark, 25°C: 225% activation, 45°C: 315% activation/wet heat, light, 25°C: 368% activation, 45°C: 687% activation
phosphoenolpyruvate
-
free, allosteric activator
Polyethylene glycol
-
required for maximal activity
pyruvate
Coccochloris peniocystis
-
activates
succinate
1 mM, 124% of initial activity
thidiazuron
-
synthetic preparation exhibiting cytokinin activity: TDZ
3-Phosphoglyceric acid
-
activates
3-Phosphoglyceric acid
Coccochloris peniocystis
-
-
acetyl-CoA
-
allosteric activator, PPC activity in extracts decreases by more than 75% in assays lacking acetyl-CoA
acetyl-CoA
1 mM, 111% of initial activity
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
D-glucose 1-phosphate
-
D-glucose 1-phosphate
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
D-glucose 6-phosphate
-
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
dry heat, dark, 25°C: 253% activation, 45°C: 347% activation/dry heat, light, 25°C: 400% activation, 45°C: 856% activation/wet heat, dark, 25°C: 258% activation, 45°C: 400% activation/wet heat, light, 25°C: 456% activation, 45°C: 908% activation
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
allosteric activator
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
1.17fold activation of isoform Osppc4 at pH 7.3, 2.51fold activation of isoform Osppc2a at pH 7.3
D-glucose 6-phosphate
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
D-glucose 6-phosphate
-
2 mM, 2fold increase of activity of PEPC1 at pH 7.3, 1.18fold increase in activity of PEPC1 at pH 8
D-glucose 6-phosphate
activates
dihydroxyacetone phosphate
-
activates
dihydroxyacetone phosphate
-
activates at pH 7 in absence of glycerol, but has no effect under other assay conditions
dihydroxyacetone phosphate
-
isoenzyme PEPC2 is inactivated 6fold by 2.0 mM, 52% activation by isoenzyme PEPC2
dioxane
-
-
fructose 1,6-bisphosphate
-
activates
fructose 1,6-bisphosphate
-
no effect
fructose 1,6-bisphosphate
-
weak activation
fructose 6-phosphate
-
activates at pH 7 in absence of glycerol, but has no effect under other assay conditions
fructose 6-phosphate
-
activates at pH 7.8
fructose 6-phosphate
-
2 mM, 2fold increase of activity of PEPC1 at pH 7.3, 1.27fold increase in activity of PEPC1 at pH 8
glucose 1-phosphate
-
activates at pH 7 in absence of glycerol, but has no effect under other assay conditions
glucose 1-phosphate
-
activates at pH 7.8
glucose 1-phosphate
-
2 mM, 1.64fold increase of activity of PEPC1 at pH 7.3, 1.07fold increase in activity of PEPC1 at pH 8
glucose 1-phosphate
Thermostichus vulcanus
slight stimulation
glucose 1-phosphate
-
weak activation
glucose 6-phosphate
-
desensitization by bicarbonate
glucose 6-phosphate
-
activates
glucose 6-phosphate
-
activates
glucose 6-phosphate
-
C4 plants and CAM plants
glucose 6-phosphate
-
activates at pH 7 in absence of glycerol, but has no effect under other assay conditions
glucose 6-phosphate
-
no effect
glucose 6-phosphate
-
stimulates
glucose 6-phosphate
-
activates PEPC1
glucose 6-phosphate
Thermostichus vulcanus
slight stimulation
glucose 6-phosphate
-
maximal activation at 2 mM
glucose 6-phosphate
-
activates
glucose 6-phosphate
-
significant activation
glucose 6-phosphate
-
activates wild-type enzyme
glutamine
-
activates
glutamine
-
isoenzyme PEPC1 is inactivated more than 4fold by 2 mM, 8% activation of isoenzyme PEPC2
Gly
-
-
Gly
-
significant activation
glycerol 3-phosphate
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
glycerol 3-phosphate
-
2 mM, 1.83fold increase of activity of PEPC1 at pH 7.3, 1.16fold increase in activity of PEPC1 at pH 8
glycine
-
-
glycine
-
allosteric activator
L-glucose 6-phosphate
-
-
L-glucose 6-phosphate
-
5.1fold stimulation of activity at 5 mM
propionyl-CoA
-
absolute requirement for acetyl-CoA or propionyl-CoA
propionyl-CoA
-
activates
additional information
not activated by D-glucose 6-phosphate
-
additional information
-
not activated by D-glucose 6-phosphate
-
additional information
-
the results presented indicate that both the natural cytokinin BAP and synthetic preparations exhibiting cytokinin activity (TDZ, kartolin-2, and kartolin-4) attenuate the suppression PEPK activities in wheat seedlings and mature plant leaves, associated with water deficiency
-
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0.05 - 0.22
2-phosphonooxyprop-2-enoate
0.19
CO2
wild-type enzyme
0.038 - 22.2
phosphoenolpyruvate
additional information
additional information
-
0.05
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h into the dark, pH: 8.0
0.05
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h into the light, pH: 8.0
0.06
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h in the dark, pH: 8.0
0.06
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h in the light, pH: 8.0
0.09
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h into the light, pH: 8.0
0.1
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h into the dark, pH: 8.0
0.1
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h into the light, pH: 8.0
0.12
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h into the dark, pH: 8.0
0.12
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h into the light, pH: 8.0
0.17
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h into the dark, pH: 8.0
0.21
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h into the light, pH: 8.0
0.22
2-phosphonooxyprop-2-enoate
-
leaves are collected after 5 h into the dark, pH: 8.0
0.04216
HCO3-
-
at pH 8.0 and 25°C
0.1
HCO3-
wild type enzyme
0.139
HCO3-
WP_019935846
23°C, pH not specified in the publication
0.169
HCO3-
-
at pH 8.0 and 25°C
0.21
HCO3-
wild-type, S0.5 value, pH 7.3, 30°C
0.23
HCO3-
-
pH 8.0, 25°C, enzyme from roots grown in absence of Fe2+
0.24
HCO3-
-
pH 8.0, 25°C, enzyme from roots grown in presence of Fe2+
0.24
HCO3-
wild-type, pH 8.0, 35°C
0.25
HCO3-
-
enzyme form PEPC I
0.25
HCO3-
mutant K946E, pH 8.0, 35°C
0.33
HCO3-
wild-type, S0.5 value, pH 7.3, 30°C
0.55
HCO3-
mutant enzyme Arg703Gly
0.7
HCO3-
-
enzyme form PEPC III
0.76
HCO3-
mutant K954E, pH 7.3, 30°C
0.8
HCO3-
Coccochloris peniocystis
-
-
0.8
HCO3-
wild-type, pH 7.3, 30°C
0.9
HCO3-
-
enzyme form PEPC II
1.28
HCO3-
-
isoenzyme PC-II
1.45
HCO3-
-
isoenzyme PC-I
1.6
HCO3-
Molinema dessetae
-
-
1.7
HCO3-
-
in presence of 0.04 mM acetyl-CoA
2.6
HCO3-
-
mutant enzyme N917G, at pH 8.5 and 25°C
2.8
HCO3-
-
mutant enzyme R873G, at pH 8.5 and 25°C
2.8
HCO3-
-
wild type enzyme, at pH 8.5 and 25°C
2.9
HCO3-
-
mutant enzyme S869G, at pH 8.5 and 25°C
3.1
HCO3-
-
mutant enzyme K813G, at pH 8.5 and 25°C
3.3
HCO3-
-
mutant enzyme R620G, at pH 8.5 and 25°C
3.5
HCO3-
-
mutant enzyme K653G, at pH 8.5 and 25°C
6.5
HCO3-
mutant enzyme Arg703Gly/Arg704Gly
0.038
phosphoenolpyruvate
-
at pH 8.0 and 25°C
0.04
phosphoenolpyruvate
-
isoform Osppc2a, at pH 8.0 and 30°C
0.047
phosphoenolpyruvate
-
isoenzyme PC-II
0.054
phosphoenolpyruvate
-
isozyme PPC1, at pH 8.5
0.06
phosphoenolpyruvate
-
pH 8.3
0.06
phosphoenolpyruvate
-
pH 8, PEPC1
0.06
phosphoenolpyruvate
-
pH 8, PEPC2
0.06
phosphoenolpyruvate
in the presence of 2 mM Mg2+, in 50 mM HEPES-NaOH buffer (pH 7.2), at 37°C
0.065
phosphoenolpyruvate
-
extract from germinated seed
0.068
phosphoenolpyruvate
-
pH 7.8, enzyme from mesocarp, stored in 20% CO2
0.069
phosphoenolpyruvate
-
pH 8.0, 25°C, enzyme from roots grown in presence of Fe2+
0.07
phosphoenolpyruvate
wild-type, S0.5 value, Hill coefficient 1.63, pH 8.0, 30°C
0.08
phosphoenolpyruvate
-
pH 8.4, 24°C, pH 7.3, 24°C, enzyme from cells grown in presence of phosphate or in absence of phosphate, assay in presence of glycerol
0.09
phosphoenolpyruvate
-
enzyme form PEPC I
0.09
phosphoenolpyruvate
-
golden delicious, vascular bundle or seed
0.09
phosphoenolpyruvate
pH 8.0, 80°C
0.09
phosphoenolpyruvate
-
desalted extracts from de-embryonated dry seed at pH 8
0.091
phosphoenolpyruvate
-
pH 8.0, 25°C, enzyme from roots grown in absence of Fe2+
0.1
phosphoenolpyruvate
-
with Mn2+ as activator
0.1
phosphoenolpyruvate
-
isoenzyme PC-I
0.1
phosphoenolpyruvate
wild-type, pH 8.0, 35°C
0.108
phosphoenolpyruvate
-
with Mg2+ as activator
0.12
phosphoenolpyruvate
-
pH 7.3, PEPC1
0.12
phosphoenolpyruvate
-
pH 7.3, PEPC2
0.12
phosphoenolpyruvate
-
pH 7.8, enzyme from mesocarp, stored in air
0.125
phosphoenolpyruvate
-
-
0.14
phosphoenolpyruvate
-
pH 7.3, no addition of phosphate, enzyme from light-adapted leaves
0.14
phosphoenolpyruvate
-
pH 7.8, enzyme from peel, stored in air
0.15
phosphoenolpyruvate
-
enzyme form PEPC III
0.15
phosphoenolpyruvate
-
cox's orange Pippin, vascular bundle
0.15
phosphoenolpyruvate
-
pH 7.3, 24°C, pH 7.3, 24°C, enzyme from cells grown in absence of phosphate, assay in presence of glycerol
0.15
phosphoenolpyruvate
-
pH 8.4, 24°C, enzyme from cells grown in presence of phosphate, assay in absence of glycerol
0.16
phosphoenolpyruvate
-
pH 8.4, 24°C, enzyme from cells grown in absence of phosphate, assay in absence of glycerol
0.16
phosphoenolpyruvate
-
isoform Osppc2a, at pH 7.3 and 30°C
0.17
phosphoenolpyruvate
-
cox's orange Pippin, seeds
0.17
phosphoenolpyruvate
-
pH 7.3, 24°C, pH 7.3, 24°C, enzyme from cells grown in presence of phosphate, assay in presence of glycerol
0.18
phosphoenolpyruvate
-
enzyme form PEPC II
0.18
phosphoenolpyruvate
-
pH 7.3, addition of 30 mM phosphate, enzyme from light-adapted leaves
0.18
phosphoenolpyruvate
-
dephospho-PEPC2
0.18
phosphoenolpyruvate
-
phosphorylated isozyme PPC, at pH 7.3
0.18
phosphoenolpyruvate
N-terminal replacement mutant, S0.5 value, Hill coefficient 1.77, pH 7.3, 30°C
0.19
phosphoenolpyruvate
wild-type enzyme
0.19
phosphoenolpyruvate
wild type enzyme, and mutant enzyme Arg703Gly/Arg704Gly
0.19
phosphoenolpyruvate
wild-type, S0.5 value, Hill coefficient 1.52, pH 7.3, 30°C
0.2
phosphoenolpyruvate
-
pH 8.2, enzyme from water stressed plants
0.21
phosphoenolpyruvate
-
-
0.21
phosphoenolpyruvate
-
-
0.23
phosphoenolpyruvate
-
in presence of 0.04 mM acetyl-CoA
0.23
phosphoenolpyruvate
-
pH 8.2
0.25
phosphoenolpyruvate
-
leaf
0.29
phosphoenolpyruvate
-
-
0.29
phosphoenolpyruvate
mutant enzyme Arg703Gly
0.29
phosphoenolpyruvate
-
stem
0.3
phosphoenolpyruvate
-
-
0.33
phosphoenolpyruvate
-
pH 7.3, no addition of phosphate, enzyme from dark-adapted leaves
0.34
phosphoenolpyruvate
-
dephosphorylated isozyme PPC1, at pH 7.3
0.34
phosphoenolpyruvate
wild-type, pH 7.3, 30°C
0.35
phosphoenolpyruvate
-
pH 7
0.4
phosphoenolpyruvate
-
pH 7.3
0.41
phosphoenolpyruvate
-
pH 7.3, 24°C, enzyme from cells grown in presence of phosphate, assay in absence of glycerol
0.42
phosphoenolpyruvate
-
pH 7.3, 24°C, enzyme from cells grown in absence of phosphate, assay in absence of glycerol
0.44
phosphoenolpyruvate
-
-
0.46
phosphoenolpyruvate
-
-
0.49
phosphoenolpyruvate
-
-
0.49
phosphoenolpyruvate
-
pH 7.3, addition of 30 mM phosphate, enzyme from dark-adapted leaves
0.55
phosphoenolpyruvate
-
phospho-PEPC2
0.55
phosphoenolpyruvate
-
phosphoPEPC1
0.55
phosphoenolpyruvate
Thermosynechococcus vestitus
-
pH 8.3, 23°C
0.56
phosphoenolpyruvate
wild-type, S0.5 value, Hill coeffcient 2.39, pH 8.0, 30°C
0.6
phosphoenolpyruvate
-
-
0.6
phosphoenolpyruvate
Coccochloris peniocystis
-
-
0.6 - 6
phosphoenolpyruvate
-
mutant enzyme R873G, at pH 8.5 and 25°C
0.62
phosphoenolpyruvate
-
wild type enzyme, at pH 8.5 and 25°C
0.64
phosphoenolpyruvate
-
-
0.64
phosphoenolpyruvate
wild-type, presence of glucose 6-phosphate, S0.5 value, Hill coeffcient 1.84, pH 7.3, 30°C
0.68
phosphoenolpyruvate
-
mutant enzyme S869G, at pH 8.5 and 25°C
0.69
phosphoenolpyruvate
-
mutant enzyme N917G, at pH 8.5 and 25°C
0.7
phosphoenolpyruvate
-
in absence of effectors, at 25°C
0.74
phosphoenolpyruvate
-
-
0.74
phosphoenolpyruvate
-
wild type enzyme, at pH 7.3 and 25°C
0.74
phosphoenolpyruvate
wild-type, S0.5 value, Hill coeffcient 2.06, pH 7.3, 30°C
0.76
phosphoenolpyruvate
-
wild type enzyme, at pH 8.0 and 25°C
0.76
phosphoenolpyruvate
K119EA mutant, presence of glucose 6-phosphate, S0.5 value, Hill coefficient 2.00, pH 7.3, 30°C
0.78
phosphoenolpyruvate
-
mutant enzyme K813G, at pH 8.5 and 25°C
0.79
phosphoenolpyruvate
-
C3 extract, light-harvested PEPC in the absence of D-glucose 6-phosphate
0.79
phosphoenolpyruvate
-
at pH 8.0 and 25°C
0.79
phosphoenolpyruvate
mutant S12D, presence of glucose 6-phosphate, S0.5 value, Hill coeffcient 1.64, pH 7.3, 30°C
0.8
phosphoenolpyruvate
mutant K946E, pH 8.0, 35°C
0.82
phosphoenolpyruvate
mutant K954E, pH 7.3, 30°C
0.83
phosphoenolpyruvate
mutant S12D, S0.5 value, Hill coeffcient 1.10, pH 7.3, 30°C
0.84
phosphoenolpyruvate
at pH 7.3
0.86
phosphoenolpyruvate
-
pH 7.2, enzyme from water stressed plants
0.87
phosphoenolpyruvate
at pH 8.0
0.92
phosphoenolpyruvate
-
dephosphoPEPC1
0.92
phosphoenolpyruvate
-
C3 extract, dark-harvested PEPC in the absence of D-glucose 6-phosphate
1
phosphoenolpyruvate
-
mutant enzyme S425A/S451D, at pH 7.3 and 25°C
1.03
phosphoenolpyruvate
-
isoform Osppc4, at pH 8.0 and 30°C
1.05
phosphoenolpyruvate
-
-
1.1
phosphoenolpyruvate
-
without activator
1.1
phosphoenolpyruvate
-
pH 8.0
1.22
phosphoenolpyruvate
WP_019935846
23°C, pH not specified in the publication
1.25
phosphoenolpyruvate
-
pH 7.2
1.3
phosphoenolpyruvate
-
-
1.6
phosphoenolpyruvate
-
mutant enzyme S425A/S451D, at pH 8.0 and 25°C
1.7
phosphoenolpyruvate
-
at 14°C
1.7
phosphoenolpyruvate
wild-type, pH 8.5, 25°C
1.89
phosphoenolpyruvate
-
C3 extract, light-harvested PEPC in the presence of 5 mM D-glucose 6-phosphate
2
phosphoenolpyruvate
-
-
2
phosphoenolpyruvate
-
isoform Osppc4, at pH 7.3 and 30°C
2
phosphoenolpyruvate
50°C, pH not specified in the publication
2
phosphoenolpyruvate
-
mutant enzyme S425A, at pH 7.3 and 25°C
2.1
phosphoenolpyruvate
-
mutant enzyme S451D, at pH 7.3 and 25°C
2.26
phosphoenolpyruvate
-
C3 extract, dark-harvested PEPC in the presence of 5 mM D-glucose 6-phosphate
2.38
phosphoenolpyruvate
Molinema dessetae
-
-
2.4
phosphoenolpyruvate
-
at 40°C
2.4
phosphoenolpyruvate
-
mutant enzyme S451D, at pH 8.0 and 25°C
2.6
phosphoenolpyruvate
-
-
2.7
phosphoenolpyruvate
-
mutant enzyme S425A, at pH 8.0 and 25°C
3.31
phosphoenolpyruvate
-
mutant enzyme K653G, at pH 8.5 and 25°C
4.88
phosphoenolpyruvate
-
mutant enzyme R620G, at pH 8.5 and 25°C
5
phosphoenolpyruvate
-
-
8.7
phosphoenolpyruvate
-
pH 7.0
8.8
phosphoenolpyruvate
mutant K653R, pH 8.5, 25°C
22.2
phosphoenolpyruvate
mutant K653Q, pH 8.5, 25°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
Panicum schenckii
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
Sorghum sp.
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
enzyme extract from plants after a 12 h dark period or a 12 h light period depending on pH
-
additional information
additional information
K0.5 (phosphoenolpyruvate) (without 5 mM glucose 6-phosphate): 0.036 mM, K0.5 (phosphoenolpyruvate) (+ 5 mM glucose 6-phosphate): 0.013 mM
-
additional information
additional information
-
K0.5 (phosphoenolpyruvate) (without 5 mM glucose 6-phosphate): 0.036 mM, K0.5 (phosphoenolpyruvate) (+ 5 mM glucose 6-phosphate): 0.013 mM
-
additional information
additional information
K0.5 (phosphoenolpyruvate) (without 5 mM glucose 6-phosphate): 0.042 mM, K0.5 (phosphoenolpyruvate) (+ 5 mM glucose 6-phosphate): 0.025 mM
-
additional information
additional information
K0.5 (phosphoenolpyruvate) (without 5 mM glucose 6-phosphate): 0.157 mM, K0.5 (phosphoenolpyruvate) (+ 5 mM glucose 6-phosphate): 0.02 mM
-
additional information
additional information
-
K0.5 (phosphoenolpyruvate) (without 5 mM glucose 6-phosphate): 0.157 mM, K0.5 (phosphoenolpyruvate) (+ 5 mM glucose 6-phosphate): 0.02 mM
-
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0.103 - 0.307
(+)-catechin
0.00196 - 0.0326
(3-bromophenyl)-4-(3-hydroxybenzylidene)-pyrazolidine-3,5-dione
0.065
2-(4-methoxyphenyl)-3-phenyl-quinoxaline
Flaveria trinervia
at pH 8.0 and 25°C
0.039
AG 1433
Flaveria trinervia
at pH 8.0 and 25°C
0.103
(+)-catechin
Flaveria trinervia
at pH 8.0 and 25°C
0.307
(+)-catechin
Flaveria pringlei
at pH 8.0 and 25°C
0.00196
(3-bromophenyl)-4-(3-hydroxybenzylidene)-pyrazolidine-3,5-dione
Flaveria trinervia
pH 7.5, 25°C
0.0326
(3-bromophenyl)-4-(3-hydroxybenzylidene)-pyrazolidine-3,5-dione
Flaveria pringlei
pH 7.5, 25°C
0.32
aspartate
Ricinus communis
-
IC50 of dephospho-PEPC1: 0.32 mM
0.35
aspartate
Ricinus communis
-
IC50 of phospho-PEPC1: 0.35 mM
2.6
aspartate
Ricinus communis
-
IC50 of phospho-PEPC2: 2.6 mM
4.5
aspartate
Ricinus communis
-
IC50 of dephospho-PEPC2: 4.5 mM, enzyme form PEPC2
2.1
glutamate
Ricinus communis
-
IC50 of phospho-PEPC1: 2.1 mM
2.2
glutamate
Ricinus communis
-
IC50 of dephospho-PEPC1: 2.2 mM
4.1
glutamate
Ricinus communis
-
IC50 of phospho-PEPC2: 4.1 mM
7
glutamate
Ricinus communis
-
IC50 of dephospho-PEPC2: 7.0 mM, enzyme form PEPC2
0.07
L-aspartate
Oryza sativa Japonica Group
pH 7.3, 30°C
0.52
L-aspartate
Arabidopsis thaliana
-
dephosphorylated isozyme PPC1
1.14
L-aspartate
Arabidopsis thaliana
-
phosphorylated isozyme PPC1
13.2
L-aspartate
Oryza sativa Japonica Group
pH 7.3, 30°C
33
L-aspartate
Ricinus communis
at pH 7.0
0.39
L-glutamate
Oryza sativa Japonica Group
pH 7.3, 30°C
7.78
L-glutamate
Oryza sativa Japonica Group
pH 7.3, 30°C
0.03
L-malate
Oryza sativa Japonica Group
pH 7.3, 30°C
0.06
L-malate
Oryza sativa
-
isoform Osppc2a, at pH 7.3 and 30°C
0.07
L-malate
Fagus sylvatica
-
leaf
0.075
L-malate
Sorghum bicolor
-
the inhibition by 0.16 mM L-malate, pH 7.3, decreases from 70 to 30%, along with a consistent increase in IC50 from 0.075 mM to 0.22 mM after 5 days of germination
0.11
L-malate
Fagus sylvatica
-
stem
0.2
L-malate
Arabidopsis thaliana
-
-
0.23
L-malate
Bienertia sinuspersici
-
samples are taken after 5 h into the dark, pH 7.2, 0.055 mM PEP
0.26
L-malate
Suaeda eltonica
-
samples are taken after 5 h in the dark, pH 7.2, 0.1 mM PEP
0.29
L-malate
Oryza sativa Japonica Group
pH 8.0, 30°C
0.3
L-malate
Arabidopsis thaliana
-
dephosphorylated isozyme PPC1
0.33
L-malate
Suaeda aralocaspica
-
samples are taken after 5 h in the dark, pH 7.2, 0.1 mM PEP
0.35
L-malate
Oryza sativa Japonica Group
pH 7.3, 30°C
0.47
L-malate
Haloxylon persicum
-
samples are taken after 5 h in the dark, pH 7.2, 0.1 mM PEP
0.6
L-malate
Bienertia sinuspersici
-
samples are taken after 5 h into the light, pH 7.2, 0.055 mM PEP
0.68
L-malate
Arabidopsis thaliana
-
phosphorylated isozyme PPC1
0.69
L-malate
Suaeda aralocaspica
-
samples are taken after 5 h in the light, pH 7.2, 0.1 mM PEP
0.7
L-malate
Oryza sativa
-
isoform Osppc4, at pH 7.3 and 30°C
0.89
L-malate
Suaeda eltonica
-
samples are taken after 5 h in the light, pH 7.2, 0.1 mM PEP
1.25
L-malate
Xylosalsola richteri
-
samples are taken after 5 h in the dark, pH 7.2, 0.1 mM PEP
1.91
L-malate
Haloxylon persicum
-
samples are taken after 5 h in the light, pH 7.2, 0.1 mM PEP
2
L-malate
Bienertia sinuspersici
-
samples are taken after 5 h into the dark, pH 7.2, 0.1 mM PEP
2.17
L-malate
Xylosalsola richteri
-
samples are taken after 5 h in the light, pH 7.2, 0.1 mM PEP
2.22
L-malate
Bienertia sinuspersici
-
samples are taken after 5 h into the light, pH 7.2, 0.1 mM PEP
3.84
L-malate
Annona cherimola
-
IC50: 3.84 mM for enzyme from mesocarop, stored in air, 5.95 mM for enzyme from mesocarop stored in 20% CO2, 2.01 mM for enzyme from peel stored in air
3.9
L-malate
Suaeda linifolia
-
samples are taken after 5 h in the dark, pH 7.2, 0.1 mM PEP
3.93
L-malate
Suaeda linifolia
-
samples are taken after 5 h in the light, pH 7.2, 0.1 mM PEP
11
L-malate
Ricinus communis
at pH 7.0
12.6
L-malate
Oryza sativa Japonica Group
pH 8.0, 30°C
0.0000026
malate
Flaveria pringlei
wild type enzyme, pH and temperature not specified in the publication
0.029
malate
Ricinus communis
-
IC50 of dephospho-PEPC1: 0.029 mM
0.075
malate
Ricinus communis
-
IC50 of phospho-PEPC1: 0.075 mM
0.2
malate
Hydrilla verticillata
-
harvest period: dark
0.4
malate
Hydrilla verticillata
-
harvest period: light
0.57
malate
Ricinus communis
-
IC50 of phospho-PEPC2: 0.57 mM
1.47
malate
Ricinus communis
-
, IC50 of dephospho-PEPC2: 1.47 mM, enzyme form PEPC2
4.3
malate
Flaveria pringlei
mutant enzyme R884Q, pH and temperature not specified in the publication
6.6
malate
Flaveria pringlei
mutant enzyme R884S, pH and temperature not specified in the publication
8
malate
Digitaria sanguinalis
-
IC50: 8 mM for PEPC activity in situ, 1.5 mM for PEPC activity in vitro
8.7
malate
Flaveria trinervia
-
wild type enzyme, pH and temperature not specified in the publication
15.7
malate
Flaveria pringlei
mutant enzyme R884E, pH and temperature not specified in the publication
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0.0018
50°C, pH not specified in the publication
0.0047
-
lutescens 758, seedlings: after stress, 1 day, without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.00521
-
lutescens 758, seedlings: after rehydration and after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.00527
-
lutescens 758, seedlings: after rehydration and without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.00536
-
lutescens 758, seedlings: after stress, 1 day, and after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.00773
-
lutescens 758, seedlings: after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.00883
-
lutescens 758, seedlings: without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.01199
-
lutescens 758, leaves: after rehydration and without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.012
-
photosynthetic rate: C3, harvest period: light, + 5 mM malate
0.01437
-
lutescens 758, leaves: after stress, 2 weeks, without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.01518
-
Mironovskaya 808 leaves: stress, 1 day, and with N-isopropoxycarbonyl-O-4-chlorophenylcarbamoyl-ethanolamine treatment
0.01525
-
Mironovskaya 808 leaves: stress, 1 day, and with 6-benzylaminopurine treatment
0.0153
-
Mironovskaya 808 leaves: control (without any treatment)
0.01559
-
Mironovskaya 808 leaves: stress, 1 day, and without any treatment
0.016
-
photosynthetic rate: C3, harvest period: dark, + 5 mM malate
0.01601
-
Mironovskaya 808 leaves: stress, 1 day, and with tidiazuron
0.01819
-
lutescens 758, leaves: after stress, 2 weeks, and after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.019
-
photosynthetic rate: C3, harvest period: light, + 5 mM malate and + 5 mM D-glucose 6-phosphate
0.01924
-
lutescens 758, leaves: after rehydration and after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.02202
-
Mironovskaya 808 leaves: stress, 2 weeks, and without any treatment
0.02308
-
Mironovskaya 808 leaves: control (without any treatment)
0.02351
-
Mironovskaya 808 leaves: stress, 2 weeks, and with tidiazuron
0.02355
-
Mironovskaya 808 leaves: stress, 1 day, and with N-isopropoxycarbonyl-O-4-chlorophenylcarbamoyl-ethanolamine treatment
0.0236
-
Mironovskaya 808 leaves: stress, 2 weeks, and with 6-benzylaminopurine treatment
0.02366
-
Mironovskaya 808 leaves: rehydration, and without any treatment
0.0239
-
Mironovskaya 808 leaves: rehydration, and with tidiazuron
0.02403
-
Mironovskaya 808 leaves: stress, 2 weeks, and with N-isopropoxycarbonyl-O-4-chlorophenylcarbamoyl-ethanolamine treatment
0.02405
-
Mironovskaya 808 leaves: stress, 1 day, and with 6-benzylaminopurine treatment
0.0241
-
Mironovskaya 808 leaves: stress, 1 day, and with tidiazuron
0.02411
-
Mironovskaya 808 leaves: rehydration, and with 6-benzylaminopurine treatment
0.02422
-
Mironovskaya 808 leaves: rehydration, and with N-isopropoxycarbonyl-O-4-chlorophenylcarbamoyl-ethanolamine treatment
0.027
-
photosynthetic rate: C3, harvest period: dark, control
0.028
-
photosynthetic rate: C3, harvest period: dark, + 5 mM malate and + 5 mM D-glucose 6-phosphate
0.029
-
with 7.5 mM NH4Cl
0.03308
-
lutescens 758, leaves: without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.03381
-
lutescens 758, leaves: after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.034
-
clarified extract, at pH 8.5
0.04
-
with phosphate treatment, pH: 4.5, malate inhibition ratio: 0.68
0.05
-
with phosphate treatment, pH: 5.0, malate inhibition ratio: 0.54
0.052
-
photosynthetic rate: C3, harvest period: light, + 5 mM D-glucose 6-phosphate
0.067
-
photosynthetic rate: C3, harvest period: dark, + 5 mM D-glucose 6-phosphate
0.11
-
no phosphate treatment, pH: 4.0, malate inhibition ratio: 0.72
0.13
-
no phosphate treatment, pH: 4.0, malate inhibition ratio: 0.59
0.134
-
photosynthetic rate: C3, harvest period: dark, + 5 mM malate
0.15
-
no phosphate treatment, pH: 5.0, malate inhibition ratio: 0.65
0.16
-
no phosphate treatment, pH: 4.5, malate inhibition ratio: 0.69
0.17
-
photosynthetic rate: C4, harvest period: light, + 5 mM malate
0.213
-
photosynthetic rate: C3, harvest period: dark, control
0.326
-
photosynthetic rate: C4, harvest period: light, control
0.374
-
photosynthetic rate: C4, harvest period: light, + 5 mM malate and + 5 mM D-glucose 6-phosphate
0.433
-
photosynthetic rate: C4, harvest period: light, + 5 mM D-glucose 6-phosphate
0.449
-
photosynthetic rate: C3, harvest period: dark, + 5 mM malate and + 5 mM D-glucose 6-phosphate
0.461
-
photosynthetic rate: C3, harvest period: dark, + 5 mM D-glucose 6-phosphate
0.7
mutant K653Q, pH 8.5, 25°C
0.913
-
PEPC activity (micromol/mg chlorophyll/min) in Chinese common Japonica rice cultivar 9516 (female parent)
107
cytosolic fraction, pH 7.5, 25°C
11
-
dark-adapted enzyme form
13.52
-
PEPC activity (micromol/mg chlorophyll/min) in JAAS45 pure diploid lines (obtained by anther culture from F1 hybrids)
14.55
Molinema dessetae
-
-
15.78
-
PEPC activity (micromol/mg chlorophyll/min) in the forth generation of JAAS45
21.8
WP_019935846
23°C, pH not specified in the publication
22.3
-
after 660fold purification, at pH 8.5
22.73
-
PEPC activity (micromol/mg chlorophyll/min) in PEPC transgenic rice germplasm (PC) (male parent)
23.7
wild-type, pH 8.5, 25°C
25.2
after 152fold purification
4.4
-
with phosphate treatment, pH: 4.0, malate inhibition ratio: 0.54
41.7
-
at pH 8.0 and 25°C
5.32
-
with phosphate treatment, pH: 4.5, malate inhibition ratio: 0.49
5.8
-
with phosphate treatment, pH: 5.0, malate inhibition ratio: 0.43
8.46
-
no phosphate treatment, pH: 4.0, malate inhibition ratio: 0.33
8.87
Coccochloris peniocystis
-
-
9.15
-
no phosphate treatment, pH: 4.5, malate inhibition ratio: 0.24
9.4
mutant K653R, pH 8.5, 25°C
9.51
-
no phosphate treatment, pH: 5.0, malate inhibition ratio: 0.58
0.002
-
in a coupled assay with malate dehydrogenase
0.002
-
in a coupled assay with malate dehydrogenase
0.023
-
photosynthetic rate: C3, harvest period: light, control
0.023
-
Mironovskaya 808 leaves: stress, 1 day, and without any treatment
0.09
-
with phosphate treatment, pH: 4.0, malate inhibition ratio: 0.76
0.09
-
with phosphate treatment, pH: 4.0, malate inhibition ratio: 0.48
0.1
-
no phosphate treatment, pH: 5.0, malate inhibition ratio: 0.49
0.1
-
with phosphate treatment, pH: 5.0, malate inhibition ratio: 0.40
0.12
-
with phosphate treatment, pH: 4.5, malate inhibition ratio: 0.44
0.12
-
no phosphate treatment, pH: 4.5, malate inhibition ratio: 0.61
21
-
-
21
-
a light-adapted enzyme form
additional information
Amaranthus edulis
-
PEPC activity is reduced to 42% and 3% of wild type activity in heterozygous and homozygous mutant plants, respectively
additional information
-
dry heat 25°C, dark: 450 micromol/mg/chlorophyll/h, light: 944 micromol/mg/chlorophyll/h
additional information
-
dry heat 45°C, dark: 705 micromol/mg/chlorophyll/h, light: 1834 micromol/mg/chlorophyll/h
additional information
-
effect of pretreatment 25°C (dark, 30 min) + 25°C (dark, 30 min): 238 micromol/mg/chlorophyll/h (none), 15.8 micromol/mg/chlorophyll/h (1 mM malate), 623 micromol/mg/chlorophyll/h (2 mM glucose-6-phosphate)
additional information
-
effect of pretreatment 25°C (dark, 30 min) + 25°C (light, 30 min): 568 micromol/mg/chlorophyll/h (none), 231 micromol/mg/chlorophyll/h (1 mM malate), 2593 micromol/mg/chlorophyll/h (2 mM glucose-6-phosphate)
additional information
-
effect of pretreatment 45°C (dark, 30 min) + 25°C (light, 30 min): 988 micromol/mg/chlorophyll/h (none), 636 micromol/mg/chlorophyll/h (1 mM malate), 8509 micromol/mg/chlorophyll/h (2 mM glucose-6-phosphate)
additional information
-
wet heat 25°C, dark: 448 micromol/mg/chlorophyll/h, light: 1069 micromol/mg/chlorophyll/h
additional information
-
wet heat 45°C, dark: 836 micromol/mg/chlorophyll/h, light: 1942 micromol/mg/chlorophyll/h
additional information
-
activity is peaking at midnight and then decreasing drastically until dawn
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
-
PEPC activity of the Brachiaria hybrid (C4 plant) leaves is 51- to 129fold higher than that estimated for wheat and rice (both C3 plants). PEPC activity in leaves and roots of the Brachiaria hybrid increases up to two-and three-fold, respectively, and decreases the malate-inhibition ratio in leaves in response to P-deficiency
additional information
-
evolution pattern of fatty acids and triacylglycerols contents is similar to that of PEPc activity, suggesting that PEPc may be involved in fatty acid and triacylglycerol biosynthesis during seed maturation
additional information
-
hybridol variety: PEPc activity does not exceed 5 micromol/h per gram of fresh weight during the first stages of maturation. It then highly increases to reach more than 30 micromol/h per gram of fresh weight
additional information
-
pactol variety: evolution of PEPc activity shows a classical curve, i.e. an increase during the most active phase of lipid accumulation in maturating seeds, followed by a rapid decrease until the end of seed maturation
additional information
-
-
additional information
-
iron deficiency responses are investigated in roots of soybean, disclosing a drastically reduced activity of the phosphoenolpyruvate carboxylase enzyme in soybean roots
additional information
-
activity is peaking during the first 2 h of darkness and then decreasing drastically until dawn
additional information
-
activity is peaking during the first 2 h of darkness and then decreasing drastically until dawn
additional information
-
it is shown that there is a positive correlation between the activation and phosphorylation states of PEPC
additional information
-
light 2 h + 0.25 mM cycloheximide : 17% of maximal enzyme activity measured, phosphorylation status: 12% /dark 2 h + 0.25 mM cycloheximide : 14% of maximal enzyme activity measured, phosphorylation status: 7%
additional information
-
light 2 h + 10 mM DTT : 38% of maximal enzyme activity measured, phosphorylation status: 29% /dark 2 h + 10 mM DTT : 4% of maximal enzyme activity measured, phosphorylation status: 0%
additional information
-
light 2 h + 50 nM akadaic acid : 88% of maximal enzyme activity measured, phosphorylation status: 99% /dark 2 h + 50 nM okadaic acid : 48% of maximal enzyme activity measured, phosphorylation status: 60%
additional information
-
light 2 h : 71% of maximal enzyme activity measured, phosphorylation status: 100% /dark 2 h : 6% of maximal enzyme activity measured, phosphorylation status: 0%
additional information
-
-
additional information
-
PEPC activity and malate-inhibition ratio are less affected in wheat and rice under P-deficiency
additional information
-
the JAAS45 pollen line exhibits high levels of PEPC activity, manifesting higher saturated photosynthetic rates, photosynthetic apparent quantum yield (AQY), photochemical efficiency of photosystem II and photochemical and non-photochemical quenching, which indicate that the JAAS45 pollen line has a high tolerance to photo-inhibition/photooxidation under strong light and high temperature
additional information
-
relative to the female parent, the produced JAAS45 pollen lines exhibit high PEPC activity (17-fold increase) and also higher photosynthetic rates (about 36%-fold increase)
additional information
the four C-terminal mutant enzymes display varying degrees of PEPC activity in vitro ranging from 23% of wild-type with the modest G961A substitution to only 0.2% for the DELTAC4-truncated form
additional information
-
-
additional information
-
PEPC activity and malate-inhibition ratio are less affected in wheat and rice under P-deficiency
additional information
higher PEPC activity in the developing grain than in flag leaf blade and glume during grain development. For 16 of the genotypes studied, the mean PEPC activity in the developing grain or glume at 15 and 25 days after flowering is significantly and positively correlated with final protein content of grain. Enzyme activities in glume and flag leaf blade are positively correlated with final grain weight but the activity in developing grain is weakly and negatively correlated with grain weight
additional information
-
-
additional information
-
ozone is able to depress PEPc activity. As compared to chambered control atmosphere, significant declines in PEPc activity by circa 26% and 32% are recorded in + 60 and + 80 atmospheres, respectively
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ear organ, protein content of grain as well as grain weight after flowering are studied in different winter wheat (Triticum aestivum L.) genotypes
brenda
-
-
brenda
PEPC1 and PEPC2 are expressed in fibres early in elongation but not in non-differentiating ovular epidermis
brenda
-
on early stages of seed development, enzyme protein is abundant in embryo and integuments, while at subsequent stages the enzyme accumulats in endosperm, nucellus and integuments. At late stages of seed development when both endosperm and nucellus are degraded, significant accumulation is observed in the embryo proper
brenda
-
brenda
the specific activity of PEPC is significantly higher than that of pyruvate kinase, PEP phosphatase, and PEP carboxykinase
brenda
-
-
brenda
ear organ
brenda
-
brenda
-
in early stages of seed development, enzyme protein is abundant in embryo and integuments, while at subsequent stages the enzyme accumulats in endosperm, nucellus and integuments
brenda
-
-
brenda
-
abaxial
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
pre-climacteric fruit
brenda
high expression level
brenda
high expression level
brenda
-
immature
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
grown photoanaerobically
brenda
-
grown photoanaerobically
-
brenda
-
grown photoanaerobically
-
brenda
-
grown photoanaerobically
brenda
-
grown photoanaerobically
-
brenda
-
grown photoanaerobically
-
brenda
-
localized in most ovular and embryonic tissues. In early stages of seed development, enzyme protein is abundant in embryo and integuments, while at subsequent stages the enzyme accumulats in endosperm, nucellus and integuments. At late stages of seed development when both endosperm and nucellus are degraded, significant accumulation is observed in the embryo proper
brenda
PPC3 is the most abundant isozyme of the developing seed, and of the embryo and the aleurone layer of germinating seeds
brenda
transcript detected
brenda
transcript detected in
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
Musa cavendishii
-
-
brenda
-
-
brenda
-
discussion of the role of the enzyme in stomatal function
brenda
-
-
brenda
-
-
brenda
weak expression detected by Northern blot-analysis
brenda
-
-
brenda
strong expression detected by Northern blot-analysis
brenda
-
-
brenda
weak expression detected by Northern blot-analysis
brenda
Amaranthus edulis
-
-
brenda
-
-
brenda
-
brenda
-
dark-adapted and light adapted
brenda
-
light-adapted
brenda
-
-
brenda
-
PEPC transcript expression rises to the peak at midnight and decreases to the minimum level at midday
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
in C4 plants, located in the mesophyll cells
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
the photosynthesis isoform Hvpepc4 is exclusively expressed in leaves during C4 induction
brenda
-
PEPC transcript expression is peaking rapidly during the first 2 h of darkness and then decreasing drastically
brenda
-
from young plants grown under controlled short-day conditions and an extraction buffer containing EDTA
brenda
-
PEPC transcript expression is peaking rapidly during the first 2 h of darkness and then decreasing drastically
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
highest expression in the leaf blade
brenda
produced at high levels in leaf mesophyll cells
brenda
-
-
brenda
-
BTPC is present in leaf buds and young expanding leaves, but undetectable in fully expanded leaves
brenda
-
-
brenda
-
brenda
-
activity and protein level of phosphoenolpyruvate carboxylase in both leaves and roots of sorghum plants increase progressively with increasing external nitrogen concentration
brenda
-
presence of ammonium increases the phosphorylation state of PEPC and PEPC kinase activity in sorghum leaves, both in light and in the dark
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
4284, 4291, 4294, 4304, 4322, 4325, 4331, 4335, 654040, 654812, 706331 brenda
-
a significant decrease in PEPc protein expression is observed in the two highest ozone-enriched treatments + 60 atmosphere and + 80 atmosphere which reduces PEPc quantity by 31% and 41%, respectively
brenda
-
isolated cell
brenda
-
-
brenda
-
BTPC shows limited expression during pollen development
brenda
-
-
brenda
-
-
brenda
only detected in
brenda
transcript detected
brenda
transcript detected in
brenda
transcripts accumulate to higher levels in roots compared to shoots, PPC3 is the main PEPC isoform expressed in Arabidopsis thaliana roots
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
Lupinus albus var. Kiev
-
-
-
brenda
-
enzyme form PEPC III
brenda
-
-
brenda
-
activity and protein level of phosphoenolpyruvate carboxylase in both leaves and roots of sorghum plants increase progressively with increasing external nitrogen concentration
brenda
-
presence of ammonium increases PEPC activity and the amount of monoubiquitinated PEPC
brenda
-
of seedlings, roots show almost double the level of PEPC activity of shoots
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
2 enzyme form: PEPC I and PEPC II
brenda
-
-
brenda
Amaranthus edulis
-
-
brenda
-
-
brenda
-
developing
brenda
-
-
brenda
-
-
brenda
-
developing. Localized in most ovular and embryonic tissues. In early stages of seed development, enzyme protein is abundant in embryo and integuments, while at subsequent stages the enzyme accumulats in endosperm, nucellus and integuments. At late stages of seed development when both endosperm and nucellus are degraded, significant accumulation is observed in the embryo proper
brenda
-
-
brenda
-
brenda
-
-
brenda
extensive transcript abundance of isoform PPC2 throughout the entire life cycle of the seed. SbPPC2 shows maximal transcript abundance at 24-48 h post-imbibition and then decreases
brenda
extensive transcript abundance of isoform PPC3 throughout the entire life cycle of the seed. PPC3 is the most abundant isozyme of the developing seed, and of the embryo and the aleurone layer of germinating seeds. PPC3 transcript levels are at maximum at the beginning of seed development, during the period of cellularization
brenda
high levels of transcripts during early development, i.e. stage I
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
occurs at low levels in roots and cotyledons of germinated seeds
brenda
-
-
brenda
-
-
brenda
-
roots show almost double the level of PEPC activity of shoots
brenda
-
-
brenda
transcripts accumulate to higher levels in roots compared to shoots
brenda
-
of seedlings, roots show almost double the level of PEPC activity of shoots
brenda
additional information
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
brenda
additional information
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
brenda
additional information
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
brenda
additional information
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
brenda
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
brenda
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
brenda
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
brenda
additional information
salt and drought exert a differential induction of PEPC gene expression in roots
brenda
additional information
salt and drought exert a differential induction of PEPC gene expression in roots. Atppc4 shows the highest induction in response to both stresses.
brenda
additional information
salt and drought exert a differential induction of PEPC gene expression in roots. Atppc4 shows the highest induction in response to both stresses.
brenda
additional information
salt and drought exert a differential induction of PEPC gene expression in roots. Atppc4 shows the highest induction in response to both stresses.
brenda
additional information
salt and drought exert a differential induction of PEPC gene expression in roots. Atppc4 shows the highest induction in response to both stresses.
brenda
additional information
-
CrPpc1/2 polypeptide levels are up-regulated as the initial supply of NH4Cl decreases from 10 to 0.5 mM. However, within 5 h after re-supply of 10 mM NH4Cl to the N-deficient cells, the CrPpc1/2 levels reverts back nearly to those observed in high-N grown cells
brenda
additional information
-
phosphoenolpyruvate carboxylase contains two isoforms in Hydrilla verticillata, hvpepc3 and hvpepc4. Transcript expression of hvpepc4 is substantially up-regulated during C4 induction, especially in the light. It is suggested that hvpepc4 encodes the C4 photosynthetic PEPC, and hvpepc3 encodes an anaplerotic form
brenda
additional information
-
no expression in epidermis, vascular bundles, or guard cells
brenda
additional information
-
BTPC is abundant in the inner integument, cotyledon, and endosperm of developing seeds
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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malfunction
Amaranthus edulis
-
the deficiency in C4 PEPC in mutant LaC4 2.16 Amaranthus edulis leaves has no effect on C3-type PEPC content and phosphorylation state in seeds, but causes impairment of energy production, thereby accounting for the reduced germination of the mutant
malfunction
-
an enzyme-deficient mutant shows severe growth defect in vitro
metabolism
-
the enzyme catalyzes catalyzes the rate-limiting step of gluconeogenesis
metabolism
-
the enzyme has a key role in carbon metabolism by fixing CO2
metabolism
-
activity and proteins levels of phosphoenolpyruvate carboxylase in both leaves and roots of sorghum plants increase progressively with increasing external nitrogen concentration
metabolism
-
analysis of temperature responses of Rubisco carboxylation and oxygenation kinetics, phosphoenolpyruvate carboxylase carboxylation kinetics, and the activity and first-order rate constant for the carbonic anhydrase hydration reaction from 10°C to 40°C using crude leaf extracts. The C4 Rubisco of Setaria viridis has a temperature response similar to measured C3 Rubisco, the Km HCO3- of phosphoenolpyruvate carboxylase increases with temperature, and large changes in cabonic anhydrase activity have minimal effect on net CO2 assimilation
metabolism
phosphoenolpyruvate metabolism, primarily catabolized by PEPC, plays a critical role in thermogenesis in Symplocarpus renifolius
metabolism
-
plants with reduced or no detectable dark phosphorylation of PepC due to reduced levels of phosphoenolpyruvate carboxylase kinase PPCK1 transcripts display up to a 66% reduction in total dark period CO2 fixation. The perturbations parallel reduced malate accumulation at dawn and decreased nocturnal starch turnover. Circadian clock control of kinase PPCK1 prolongs the activity of PepC throughout the dark period, optimizing Crassulacean acid metabolism-associated dark CO2 fixation, malate accumulation, Crassulacean acid metabolism productivity, and core circadian clock robustness
physiological function
PEPC is a key enzyme in the synthesis of malate
physiological function
-
Bradyrhizobium japonicum utilizes PPC as an anaplerotic enzyme for growth on carbon sources metabolized to three-carbon intermediates
physiological function
-
BTPC accelerates the metabolic flow for the synthesis of storage substances during pollen maturation
physiological function
-
BTPC accelerates the metabolic flow for the synthesis of storage substances during pollen maturation
physiological function
-
BTPC and thus class-2 PEPC up-regulation is a distinctive feature of rapidly growing and/or biosynthetically active tissues that require a large anaplerotic flux from phosphoenolpyruvate to replenish tricarboxylic acid cycle C-skeletons being withdrawn for anabolism
physiological function
-
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 stess acclimation, seed germination, seed development, and cell expansion
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
-
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
physiological function
Musa cavendishii
-
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
physiological function
-
the enzyme is suited for organic acid synthesis and NADH reoxidation in the mature fruit
physiological function
-
the phosphorylation status and the protein levels of PEPC are crucial in modulating the daily and seasonal patterns in C4 leaves in situ
physiological function
-
enzyme overexpression increases the number of opened stomata in dark adapted leaves
physiological function
-
the enzyme is a key player in C4 photosynthesis
physiological function
-
the phosphoenolpyruvate carboxylase gene is important for intra-erythrocytic survival of Plasmodium falciparum
physiological function
2.3 and 11.2fold overexpression at RNA level and increases the amounts of the PEPCase protein by 1.3 and 2.3fold, respectively. Addition of bicarbonate to the overexpressing lines increases biomass of the transformants by about 12% compared to wild type, and their maximum specific growth rate in exponential phase is about 10% greater than that of wild type. The transformants also exhibit higher photosynthetic productivity
physiological function
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
physiological function
a Propionibacterium freudenreichii strain expressing PepC grows significantly faster, consumes more glycerol, and produces propionate to a higher final titer at a faster rate. The strain also produces significantly more propionate from glucose under elevated CO2 partial pressure
physiological function
an isoform PPC3 mutant has a growth-arrest phenotype and is affected in phosphate and salt-stress responses
physiological function
important contribution of the SbPPC4 isogene to the cellularization stage of development (stage I) and during germination
physiological function
-
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
physiological function
-
Oryza sativa plants expressing Zea mays phosphoenolpyruvate carboxylase are taller and have a stronger stalk, wider leaves, and more exuberant root system, with increased photosynthetic enzyme activity and improved yield components
physiological function
-
Bradyrhizobium japonicum utilizes PPC as an anaplerotic enzyme for growth on carbon sources metabolized to three-carbon intermediates
-
physiological function
Lupinus albus var. Kiev
-
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
-
physiological function
-
2.3 and 11.2fold overexpression at RNA level and increases the amounts of the PEPCase protein by 1.3 and 2.3fold, respectively. Addition of bicarbonate to the overexpressing lines increases biomass of the transformants by about 12% compared to wild type, and their maximum specific growth rate in exponential phase is about 10% greater than that of wild type. The transformants also exhibit higher photosynthetic productivity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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10300
-
1 * 12500 + 6 * 60600 + 2 * 16600 + 2 * 10300, PEPC2, SDS-PAGE
104000
-
x * 104000, SDS-PAGE
10700
-
1 * 110000 + 1 * 10700 + 1 * 93000 + 1 * ?, SDS-PAGE
109000
-
x * 109000, calculation from nucleotide sequence
111000
-
4 * 111000 Determined by: 1D native-PAGE and 2D BN-/SDS-PAGE, combined with immunoblotting
112000
-
4 * 112000, SDS-PAGE
117000
-
x * 117000, recombinant enzyme, SDS-PAGE
1186000
-
PEPC3, gel filtration
120000
Thermostichus vulcanus
4 * 120000, SDS-PAGE
12500
-
1 * 12500 + 6 * 60600 + 2 * 16600 + 2 * 10300, PEPC2, SDS-PAGE
130000
-
4 * 130000, SDS-PAGE
14900
-
3 * 22100 + 2 * 14900 + 7 * 30900 + 8 * 32100, PEPC4, SDS-PAGE
1590000
-
PEPC4, gel filtration
16600
-
1 * 12500 + 6 * 60600 + 2 * 16600 + 2 * 10300, PEPC2, SDS-PAGE
19900
-
2 * 19900 + 3 * 27900 + 5 * 30600 + 4 * 21600, PEPC3, SDS-PAGE
21600
-
2 * 19900 + 3 * 27900 + 5 * 30600 + 4 * 21600, PEPC3, SDS-PAGE
22100
-
3 * 22100 + 2 * 14900 + 7 * 30900 + 8 * 32100, PEPC4, SDS-PAGE
225700
-
sucrose density gradient centrifugation, isoenzyme PC-I
270800
-
sucrose density gradient centrifugation, isoenzyme PC-II
27900
-
2 * 19900 + 3 * 27900 + 5 * 30600 + 4 * 21600, PEPC3, SDS-PAGE
280000
-
sucrose density gradient centrifugation
285000
-
enzyme from illuminated leaf extract, dimer, gel filtration
30600
-
2 * 19900 + 3 * 27900 + 5 * 30600 + 4 * 21600, PEPC3, SDS-PAGE
30900
-
3 * 22100 + 2 * 14900 + 7 * 30900 + 8 * 32100, PEPC4, SDS-PAGE
310000
-
gel filtration in presence of malate
32100
-
3 * 22100 + 2 * 14900 + 7 * 30900 + 8 * 32100, PEPC4, SDS-PAGE
340000
-
analytical ultracentrifugation
361000
-
calculation from sedimentation and diffusion measurement
370000
-
gel filtration in absence of malate
380000 - 400000
-
gel filtration
391000
-
PEPC1, gel filtration
420000
-
enzyme from illuminated leaf extract, tetramer, gel filtration
43000
-
x * 43000, SDS-PAGE
570000
Thermostichus vulcanus
gel filtration
58772
x * 58772, calculated from sequence
60600
-
1 * 12500 + 6 * 60600 + 2 * 16600 + 2 * 10300, PEPC2, SDS-PAGE
650000
-
high-molecular-weight isoenzyme PEPC2, gel filtration
669000
-
x * 669000, class-2 PEPC enzyme-forms a high-molecular-mass, hetero-oligomeric complex containing both CrPpc1 (p109) and CrPpc2 (p131) polypeptides. Determined by: 1D nativePAGE and 2D BN/SDSPAGE, combined with immunoblotting
681000
-
gel filtration, PEPC2
70680
-
predicted from cDNA
88000
-
4 * 88000, SDS-PAGE
910000
-
class-2 PEPC, gel filtration
95000
-
4 * 95000, SDS-PAGE
96000
-
x * 96000, SDS-PAGE
97000
-
x * 97000, SDS-PAGE
984000
-
PEPC2, gel filtration
99000
-
x * 99000, SDS-PAGE
100000
-
4 * 100000, SDS-PAGE
100000
Crassula argentea
-
4 * 100000, SDS-PAGE
100000
-
4 * 100000, SDS-PAGE
100000
-
4 * 100000, SDS-PAGE
100000
-
4 * 100000, isoenzyme PEPC1, SDS-PAGE
102000
-
4 * 102000, SDS-PAGE
102000
-
4 * 102000, isoform PEPC1, SDS-PAGE
102000
-
4 * 102000, PEPC1, SDS-PAGE
105000
-
x * 105000
105000
-
4 * 105000, SDS-PAGE
105000
4 * 105000, nondenaturing PAGE
107000
-
gel filtration
107000
-
4 * 107000 + 4 * 64000, PEPC2, SDS-PAGE
107000
-
4 * 107000, PEPC1, SDS-PAGE
107000
-
x * 107000 + x * 64000, enzyme form PEPC2
107000
-
4 * 107000, native enzyme, gel filtration
107000
-
4 * 107000 + 4 * 118000, class-2 PEPC, SDS-PAGE
107000
-
4 * 107000, class-1 PEPC, SDS-PAGE
107000
-
4 * 107000, PTPC, SDS-PAGE
110000
-
SDS-PAGE
110000
-
4 * 110000, SDS-PAGE
110000
-
x * 110000, SDS-PAGE
110000
-
x * 110000, SDS-PAGE
110000
-
1 * 110000 + 1 * 10700 + 1 * 93000 + 1 * ?, SDS-PAGE
118000
PPC4, gel filtration
118000
-
4 * 107000 + 4 * 118000, class-2 PEPC, SDS-PAGE
118000
-
x * 118000, BTPC, SDS-PAGE
260000
-
gel filtration
260000
-
enzyme from darkened leaf extract, dimer, gel filtration
400000
-
gel filtration
400000
Crassula argentea
-
native PAGE
400000
-
non-denaturing PAGE
400000
-
low-molecular-mass isoenzyme PEPC1, gel filtration
400000
-
calculation from sedimentation velocity
410000
-
enzyme from darkened leaf extract, tetramer, gel filtration
410000
-
gel filtration, PEPC1
410000
-
class-1 PEPC, gel filtration
430000
-
gel filtration
50000
-
4 * 50000, SDS-PAGE
560000
-
gel filtration
560000
Coccochloris peniocystis
-
gel filtration
60000
-
4 * 60000, SDS-PAGE
60000
-
4 * 60000, SDS-PAGE
64000
Molinema dessetae
-
x * 64000, SDS-PAGE in presence of 2-mercaptoethanol
64000
-
4 * 107000 + 4 * 64000, PEPC2, SDS-PAGE
64000
-
x * 107000 + x * 64000, enzyme form PEPC2
900000
-
gel filtration
900000
-
in late bicellular pollen of lily, BTPC forms a heterooctameric class-2 PEPC complex with PTPC of 900000 Da to express PEPC activity
93000
-
4 * 93000, SDS-PAGE
93000
-
1 * 110000 + 1 * 10700 + 1 * 93000 + 1 * ?, SDS-PAGE
additional information
-
-
additional information
-
sequencing of the N-terminus, peptide mapping and immunological data suggest that the catalytic subunit of the enzyme is not related to the prokaryotic enzyme and is only distantly related to higher plant C4 and C3 enzymes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
Crassula argentea
-
the enzyme exists as tetramer during the night and as a dimer during the day
heteromer
-
x * 669000, class-2 PEPC enzyme-forms a high-molecular-mass, hetero-oligomeric complex containing both CrPpc1 (p109) and CrPpc2 (p131) polypeptides. Determined by: 1D nativePAGE and 2D BN/SDSPAGE, combined with immunoblotting
heterotetramer
-
1 * 110000 + 1 * 10700 + 1 * 93000 + 1 * ?, SDS-PAGE
?
-
x * 104000, SDS-PAGE
?
-
isoenzyme PEPC2 is a complex between the PEPC catalytic subunit of MW 100000 Da and other immunologically unrelated polypeptides of 50000-700000 Da
?
-
isoenzyme PEPC2 is a complex between the PEPC catalytic subunit of MW 100000 Da and other immunologically unrelated polypeptides of 50000-700000 Da
-
?
Molinema dessetae
-
x * 64000, SDS-PAGE in presence of 2-mercaptoethanol
?
-
1 * 12500 + 6 * 60600 + 2 * 16600 + 2 * 10300, PEPC2, SDS-PAGE
?
WP_019935846
x * 98000, SDS-PAGE
?
-
x * 117000, recombinant enzyme, SDS-PAGE
?
-
x * 99000, SDS-PAGE
-
?
-
x * 118000, BTPC, SDS-PAGE
?
x * 58772, calculated from sequence
?
-
x * 58772, calculated from sequence
-
?
-
x * 109000, calculation from nucleotide sequence
?
-
x * 43000, SDS-PAGE
-
heterooctamer
-
in late bicellular pollen of lily, BTPC forms a heterooctameric class-2 PEPC complex with PTPC to express PEPC activity
heterooctamer
-
4 * 107000 + 4 * 118000, class-2 PEPC, SDS-PAGE
homotetramer
-
4 * 107000, native enzyme, gel filtration
homotetramer
-
4 * 111000 Determined by: 1D native-PAGE and 2D BN-/SDS-PAGE, combined with immunoblotting
homotetramer
-
4 * 102000, isoform PEPC1, SDS-PAGE
homotetramer
4 * 105000, nondenaturing PAGE
homotetramer
-
4 * 107000
homotetramer
-
4 * 107000, class-1 PEPC, SDS-PAGE
homotetramer
-
4 * 107000, PTPC, SDS-PAGE
homotetramer
-
4 * 60000, SDS-PAGE
homotetramer
-
4 * 60000, SDS-PAGE
-
octamer
-
4 * 107000 + 4 * 64000, PEPC2, SDS-PAGE
octamer
-
x * 107000 + x * 64000, enzyme form PEPC2
tetramer
-
4 * 100000, SDS-PAGE
tetramer
-
4 * 100000, isoenzyme PEPC1, SDS-PAGE
tetramer
-
4 * 100000, isoenzyme PEPC1, SDS-PAGE
-
tetramer
-
4 * 50000, SDS-PAGE
tetramer
X-ray crystallography, analytical ultracentrifugation, or sedimentation velocity analysis
tetramer
Crassula argentea
-
the enzyme exists as tetramer during the night and as a dimer during the day
tetramer
Crassula argentea
-
4 * 100000, SDS-PAGE
tetramer
-
4 * 100000, SDS-PAGE
tetramer
-
4 * 93000, SDS-PAGE
tetramer
-
4 * 93000, SDS-PAGE
-
tetramer
-
4 * 88000, SDS-PAGE
tetramer
-
4 * 105000, SDS-PAGE
tetramer
-
4 * 112000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
2 * 19900 + 3 * 27900 + 5 * 30600 + 4 * 21600, PEPC3, SDS-PAGE
tetramer
-
3 * 22100 + 2 * 14900 + 7 * 30900 + 8 * 32100, PEPC4, SDS-PAGE
tetramer
-
4 * 102000, PEPC1, SDS-PAGE
tetramer
-
4 * 102000, SDS-PAGE
tetramer
-
4 * 102000, SDS-PAGE
-
tetramer
-
4 * 102000, SDS-PAGE
-
tetramer
-
4 * 107000, PEPC1, SDS-PAGE
tetramer
-
4 * 130000, SDS-PAGE
tetramer
-
4 * 95000, SDS-PAGE
tetramer
Thermostichus vulcanus
4 * 120000, SDS-PAGE
tetramer
-
4 * 100000, SDS-PAGE
tetramer
-
4 * 110000, SDS-PAGE
additional information
Crassula argentea
-
dilution induces a dissociation of the native tetramer to a less active dimer, preincubation of the dilute enzyme with phosphoenolpyruvate stabilizes the tetramer while the presence of malate induces dimer formation, glucose 6-phosphate induces tetramer formation of the dilute enzyme, both the substrate phosphoenolpyruvate and the activator glucose 6-phosphate stabilize the active tetramer via binding and interaction at an activator site separate from the active site
additional information
-
concentration-dependent dissociation of tetrameric into dimeric forms
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additional information
-
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
-
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
-
phosphoprotein
Amaranthus edulis
-
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
-
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
-
PEPC is phosphorylated only during the dark period, especially at midnight
phosphoprotein
-
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
-
the phosphoenolpyruvate carboxylase kinase gene product PPCk1 is responsible for leaf PEPC phosphorylation
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
the enzyme may exist in a dephosphorylated form in cell grown in absence of phosphate and in cells grown in presence of phosphate
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
PEPC is phosphorylated only during the dark period, especially during the first 2 h of darkness
phosphoprotein
-
PEPC is phosphorylated only during the dark period, especially during the first 2 h of darkness
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
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
-
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
-
the protein phosphatase inhibitor, okadaic acid, promotes the phosphorylation of PEPCK
phosphoprotein
Musa cavendishii
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
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
-
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
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
phosphorylation at Ser425 is promoted during seed development, Ser425 phosphorylation results in significant bacterial-type phosphoenolpyruvate carboxylase inhibition
phosphoprotein
-
PTPC of castor oil seeds is activated by phosphorylation at Ser-11 during endosperm development
phosphoprotein
-
phosphorylated at Ser451
phosphoprotein
-
the enzyme is in vivo phosphorylated at Ser451
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
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
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
the guard cell enzyme is regulated by reversible phosphorylation of at least one isoform
ubiquitination
-
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
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K112E
mutation at succinylation site, does not affect glutamate production
K112R
mutation at succinylation site, does not affect glutamate production
K653G
-
the mutation dramatically reduces the enzyme activity
K653Q
acetylation mimic mutation, abolishes glutamate production. Growth is not affected
K653R
non-acylation mimic mutant, retains glutamate production, the final glutamate concentration does not reach wild-type levels. Growth is not affected
K813G
-
the mutation does not significantly alter the enzyme activity
N917G
-
the mutation does not significantly alter the enzyme activity and results in about 37% improved L-lysine production
R620G
-
the mutation dramatically reduces the enzyme activity
R873G
-
the mutation does not significantly alter the enzyme activity
S869G
-
the mutation does not significantly alter the enzyme activity
K112E
-
mutation at succinylation site, does not affect glutamate production
-
K112R
-
mutation at succinylation site, does not affect glutamate production
-
K653Q
-
acetylation mimic mutation, abolishes glutamate production. Growth is not affected
-
K653R
-
non-acylation mimic mutant, retains glutamate production, the final glutamate concentration does not reach wild-type levels. Growth is not affected
-
K653G
-
the mutation dramatically reduces the enzyme activity
-
N917G
-
the mutation does not significantly alter the enzyme activity and results in about 37% improved L-lysine production
-
R620G
-
the mutation dramatically reduces the enzyme activity
-
R873G
-
the mutation does not significantly alter the enzyme activity
-
S869G
-
the mutation does not significantly alter the enzyme activity
-
R438C
Arg438Cys has an increased tendency to dissociate into dimers. Mutant enzyme Arg703Gly shows a 5fold decreased turnover number compared to the wild type enzyme
R703G/R703G
mutant enzyme Arg703Gly/Arg704Gly shows a 20fold decreased turnover number compared to the wild type enzyme
R884E
the mutant is clearly less sensitive towards malate compared to the wild type enzyme
R884Q
the mutant is clearly less sensitive towards malate compared to the wild type enzyme
R884S
the mutant is clearly less sensitive towards malate compared to the wild type enzyme
E946K
mutation renders the enzyme sensitive to inhibition by malate, aspartate, and fumarate
S12D
mutation of phosphorylatable serine
S425A
-
the mutant shows strongly increased Km values compared to the wild type enzyme
S425A/S451D
-
the mutant shows strongly increased Km values compared to the wild type enzyme
S451D
-
the mutant shows strongly increased Km values compared to the wild type enzyme
delataC1
deletion of the last c-terminal amino acid. kcat: 9.5/sec (phosphoenolpyruvate),12.6% of wild type catalytic activity
delataC4
deletion of the last 4 c-terminal amino acids. kcat: 0.174/sec (phosphoenolpyruvate), 0.14% wild type catalytic activity
G961A
kcat: 17.4/sec (phosphoenolpyruvate), 24.3% of wild type catalytic activity
G961V
kcat: 7.2/sec (phosphoenolpyruvate), 8.5% of wild type catalytic activity
S8C
Sorghum sp.
-
he S-carboxymethylated S8C mutant enzyme, in contrast to the SH-modified wild type protein, has an increased I0.5 value for L-malate similar to that of the phosphorylated Ser8 enzyme and the S8D mutant protein
E954K
mutation renders the enzyme sensitive to inhibition by malate, aspartate, and fumarate
D228N
-
reduced apparent affinity for the activator glycine
E229A
-
maximal activation caused by glycine is greatly reduced, significantly lowered sensitivity to the inhibitors malate and aspartate. K(0.5) for phosphoenolpyruvate is lower than wild-type value
R183Q
-
mutation results in complete desensitization to glucose 6-phosphate, heterotrophic effect of glucose 6-phosphate on the allosteric inhibitor L-malate is abolished. Sensitivity to the allosteric activator Gly is not affected
R183Q/R184Q
-
mutation results in complete desensitization to glucose 6-phosphate
R184Q
-
mutation results in complete desensitization to glucose 6-phosphate
R226Q
-
maximal activation caused by glycine is greatly reduced, significantly lowered sensitivity to the inhibitors malate and aspartate. K(0.5) for phosphoenolpyruvate is significantly higher than that of wild-type enzyme
R231A
-
decreased apparent affinity for the activator glucose 6-phosphate
R232Q
-
decreased apparent affinity for the activator glucose 6-phosphate, reduced apparent affinity for the activator glycine
R372Q
-
mutation results in a marked decrease in sensitivity to glucose 6-phosphate
additional information
Amaranthus edulis
-
heterozygous (Pp) and homozygous (pp) forms of a PEPC-deficient mutant of the C4 dicot Amaranthus edulis are analysed
additional information
Amaranthus edulis
-
rates of CO2 assimilation in air drop to 78% and 10% of the wild-type values in heterozygous and homozygous mutants, respectively. Stomatal conductance in air (531 microbar CO2) is similar in the wild-type and heterozygous mutant but the homozygous mutant has only 41% of the wild-type steady-state conductance under white light and the stomata opens more slowly in response to increased light or reduced CO2 partial pressure, suggesting that the C4 PEPC isoform plays an essential role in stomatal opening. Little difference in delta13C between the heterozygous mutant and wild type, indicating that leakiness, the ratio of CO2 leak rate out of the bundle sheath to the rate of CO2 supply by the C4 cycle, a measure of the coordination of C4 photosynthesis, is not affected by a 60% reduction in PEPC activity
additional information
at the rapid elongation phase of 10 days after anthesis, the PEPC activity in the monogenic, dominant cotton mutant Ligon lintless is only 25% of the wild type, which corresponded to about 55% reduction of fibre length
additional information
-
at the rapid elongation phase of 10 days after anthesis, the PEPC activity in the monogenic, dominant cotton mutant Ligon lintless is only 25% of the wild type, which corresponded to about 55% reduction of fibre length
additional information
-
replacement of the N-terminal 25 residues of Ppc2a with the 27 N-terminal residues of chloroplastic isoform Ppc4 reduces Vmax value to 75% and markedly affects the sensitivities to aspartate and glutamate. When K119 at the N-terminus of the N-terminal loop is replaced with the glutamate-alanine pair of isoform Ppc4, K119EA mutant, S0.5 for phosphoenolpyruvate of the resulting Ppc2a mutant increases 4fold relative to that of the wild type and reaches the level observed for isoform Ppc4
additional information
replacement of the N-terminal 25 residues of Ppc2a with the 27 N-terminal residues of chloroplastic isoform Ppc4 reduces Vmax value to 75% and markedly affects the sensitivities to aspartate and glutamate. When K119 at the N-terminus of the N-terminal loop is replaced with the glutamate-alanine pair of isoform Ppc4, K119EA mutant, S0.5 for phosphoenolpyruvate of the resulting Ppc2a mutant increases 4fold relative to that of the wild type and reaches the level observed for isoform Ppc4
additional information
it is shown that even a modest, neutral alteration of the PEPC C-terminal hydrogen atom side chain is detrimental to enzyme function
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-2
-
activity increases after exposition of fruits to -2°C for 4 h
0
-
45 min, 70% loss of activity without addition of stabilizing agent, 14% loss of activity in presence of 10 mM MgCl2, 8% loss of activity in presence of 4 mM phosphoenolpyruvate, 73% loss of activity in presence of 5 mM pyruvate, 41% loss of activity in presence of 6 mM L-malate, 5% loss of activity in presence of 10 mM glucose-6-phosphate
15
-
pH 7.0, in presence of 1 mM dithiothreitol
20 - 45
-
the enzyme remains stable
24
-
45 min, 12% loss of activity without addition of stabilizing agent, 1% loss of activity in presence of 10 mM MgCl2, no loss of activity in presence of 4 mM phosphoenolpyruvate, 17% loss of activity in presence of 5 mM pyruvate, no loss of activity in presence of 6 mM L-malate, no loss of activity in presence of 10 mM glucose-6-phosphate
25
-
30 min, pH 7, no loss of activity
5 - 40
-
enzyme activity remains steady in the range of 5-30°C and rapidly declines in the range of 30-40°C
55 - 57
-
10 min, 50% denaturation
60 - 65
-
rapid inactivation
67
-
10 min, inactivation
70
Thermostichus vulcanus
20 min, complete inactivation
100
-
50% loss of activity after 1 min
100
-
1 min, 50% loss of activity
30
-
30 min, pH 7, 15% loss of activity
30
-
3 min, no loss of activity, PEPC1
35
-
30 min, 40% loss of activity
35
-
3 min, 19% loss of activity, PEPC1
40
-
30 min, pH 7, 89% loss of activity
40
-
3 min, 25% loss of activity, PEPC1
40
Thermosynechococcus vestitus
-
15 min, no loss of activity
45
-
2 min, 56% loss of activity
45
-
30 min, pH 7, complete loss of activity
45
-
rapid decrease of activity above
45
-
3 min, 40% loss of activity, PEPC1
45
-
3 min, no loss of activity, PEPC2
45
-
50% inactivation after 87 s, isoenzyme PC-I. 50% inactivation after 100 s, isoenzyme PC-II
50
-
10 min, only small activity loss below 50°C
50
-
enzyme form PEPC I: complete inactivation after 15 s, enzyme forms PEPC II and PEPC III: complete inactivation after 25 s
50
-
3 min, 20% loss of activity, PEPC2
50
-
3 min, 82% loss of activity, PEPC1
50
Thermostichus vulcanus
60 min, stable
50
Thermosynechococcus vestitus
-
15 min, 84% residual activity
50
-
50% inactivation after 18 s, isoenzyme PC-I. 50% inactivation after 28 s, isoenzyme PC-II
55
-
3 min, complete loss of activity, PEPC1
55
-
3 min, complete loss of activity, PEPC2
55
-
50% inactivation after 13 s, isoenzyme PC-I. 50% inactivation after 17 s, isoenzyme PC-II
60
-
2 min, complete loss of activity
60
Thermostichus vulcanus
10 min, 50% loss of activity
60
Thermosynechococcus vestitus
-
15 min, 71% residual activity
75
-
3 min, inactivation
75
-
2 h, no loss of activity
80
-
50% loss of activity after 240 min
80
-
2 h, no loss of activity
90
-
50% loss of activity after 20 min
90
-
60 min, 50% loss of activity
95
-
10 min, 50% loss of activity
additional information
-
10 mM Mg2+ stabilizes the enzyme against cold inactivation. At low Mg2+ concentrations, 4 mM, the enzyme is strongly protected by phosphoenolpyruvate, glucose-6-phosphate, and, partially, by L-malate
additional information
-
phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37°C in plant extract
additional information
-
malate, 10 mM, protects from inactivation at 55°C, at pH 5.5, but not at pH 8.3
additional information
-
reversible loss of activity between 30°C and 45°C, may represent a temperature-dependent equilibrium between two forms of enzyme
additional information
-
phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37°C in plant extract
additional information
-
malate, 10 mM, protects from inactivation at 55°C, at pH 5.5, but not at pH 8.3
additional information
Panicum schenckii
-
phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37°C in plant extract
additional information
Panicum schenckii
-
malate, 10 mM, protects from inactivation at 55°C, at pH 5.5, but not at pH 8.3
additional information
-
phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37°C in plant extract
additional information
-
malate, 10 mM, protects from inactivation at 55°C, at pH 5.5, but not at pH 8.3
additional information
-
phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37°C in plant extract
additional information
-
malate, 10 mM, protects from inactivation at 55°C, at pH 5.5, but not at pH 8.3
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carbon metabolism is analysed in generated transgenic rice plants expressing either PEPC or both phosphoenolpyruvate carboxykinase (PCK) and PEPC: Results suggest that overexpression of PEPC enhances the anaplerotic pathway rather than the initial carbon fixation of the C4-like photosynthetic pathway, and that elevated PEPC activity in combination with PCK activity contributes little to C4-like carbon flow
-
cloned as a Histag-fusion protein in an Escherichia coli PEPC- (Ppc-) strain
cloned in Escherichia coli DH5alpha. Knock-out as well as over-expression mutants are constructed and characterized. Knocking out phosphoenolpyruvate carboxylase decreases the maximum cell density by 14% and increases the acetate excretion by 7%. Over-expression of phosphoenolpyruvate carboxylase increases the maximum cell dry weight by 91%. No acetate excretion is detected at these increased cell densities
-
cloning of ppc1 in Escherichia coli
cloning of ppc2 in Escherichia coli
codon-optimized expression in Escherichia coli
WP_019935846
expressed in Arabidopsis thaliana
-
expressed in Arabidopsis thaliana under the control of the cauliflower mosaic virus 35S promoter. SvPEPC is capable of efficiently exerting its activity in the plant cell environment so as to cause imbalance between aromatic and non-aromatic amino acid synthesis
Thermostichus vulcanus
-
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)-RIL cells
-
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
-
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIPL cells
-
expressed in Escherichia coli SGJS117
-
expressed in Escherichia coli strains BL21(DE) and BL21-Gold(DE)
expressed in Escherichia coli with an N-terminal His-tag
expressed in Nicotiana tabacum BY-2 cells
-
expressed in Sinorhizobium meliloti mutant RmF991
-
expression in Escherichia coli
expression in Escherichia coli as a fusion protein, the extra 159 amino acid residues fused at the N-terminus of the enzyme protein have no effect on catalytic and regulatory properties
-
expression in Escherichia coli as a fusion with the Escherichia coli maltose-binding protein
expression in Escherichia coli BL21(DE3)pLysS
-
high level of PEPC gene is stably inherited and transferred from the male parent, PEPC transgenic rice, into a female parent, japonica rice cv. 9516. The produced JAAS45 pollen lines are more tolerant to photoinhibition and to photo-oxidative stress.
-
isozymic forms are encoded by a small gene family
-
phosphoenolpyruvate carboxylase and Lactococcus lactis pyruvate carboxylase are overexpressed in Escherichia coli concurrently to improve the production of succinate. This coexpression system is also applied to mutant strains of Escherichia coli strategically designed by inactivating the competing pathways of succinate formation. Coexpression of phosphoenolpyruvate carboxylase and Lactococcus lactis pyruvate carboxylase is effective in depleting pyruvate accumulation and increasing the production of metabolites
-
phosphoenolpyruvate carboxylase is ectopically overexpressed in Vicia narbonensis seeds: Transgenic embryos take up more carbon and nitrogen. Changes in dry to FW ratio, seed fill duration and major seed components indicate altered seed development. Array-based gene expression analysis of embryos reveals upregulation of seed metabolism, especially during the transition phase and at late maturation.
-
subcloned into the streptomycete high-copy-number plasmid vector pIJ486 and transferred into Streptomyces lividans
-
to elucidate the photosynthetic physiological characteristics and the physiological inherited traits of rice hybrids and their parents, physiological indices of photosynthetic CO2 exchange and chlorophyll fluorescence parameters are measured in leaves of the maize phosphoenolpyruvate carboxylase (PEPC) transgenic rice as the male parent, sp. japonica rice cv. 9516 as the female parent, and the stable JAAS45 pollen line. The results reveal that the PEPC gene can be stably inherited and transferred from the male parent to the JAAS45 pollen line
-
using the antisense technique the expression of Ljpepc1 is decreased in three independent transgenic Lotus japonicus plants (designated as Asppc1, Asppc2 and Asppc3). In nodules of Asppc plants, PEPC activity is reduced to about 10% of that of non-transformants and the plants show typical nitrogen-deficient symptoms without a supply of nitrogen nutrient, and returned to normal growth when nitrate was supplied at 2.5 mM. The acetylene reduction activity per fresh weight of nodules of these Asppc plants decreases by 29% at 35 days after infection
-
-
-
expressed in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strains BL21(DE) and BL21-Gold(DE)
expressed in Escherichia coli strains BL21(DE) and BL21-Gold(DE)
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
Thermostichus vulcanus
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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