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carboxylase/maïs
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Ribulose-1,5-bisphosphate carboxylase/oxygenase from Zea mays: amino-acid sequence of the small subunit.
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The amino-acid sequence of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from Zea mays has been determined by alignment of peptides generated by digestion with trypsin, chymotrypsin, staphylococcal protease and thermolysin. The protein-chemically determined structure is in
Hydrolysis of phosphoenolpyruvate catalyzed by phosphoenolpyruvate carboxylase from Zea mays.
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In addition to the normal carboxylation reaction, phosphoenolpyruvate carboxylase from Zea mays catalyzes a HCO3(-)-dependent hydrolysis of phosphoenolpyruvate to pyruvate and Pi. Two independent methods were used to establish this reaction. First, the formation of pyruvate was coupled to lactate
The impact of ozone on juvenile maize (Zea mays L.) plant photosynthesis: effects on vegetative biomass, pigmentation, and carboxylases (PEPc and Rubisco).
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The impact of ozone on crops was more studied in C (3) than in C (4) species. In C (3) plants, ozone is known to induce a photosynthesis impairment that can result in significant depressions in biomass and crop yields. To investigate the impact of O (3) on C (4) plant species, maize seedlings ( ZEA
Changes in PEP carboxylase, rubisco and rubisco activase mRNA levels from maize (Zea mays) exposed to a chronic ozone stress.
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We quantified the ozone impact on levels of Zea mays L. cv. Chambord mRNAs encoding C4-phosphoenolpyruvate carboxylase (C4-PEPc), ribulose-l,5-bisphosphate carboxylase/oxygenase small and large subunits (Rubisco-SSU and Rubisco-LSU, respectively) and Rubisco activase (RCA) using real-time RT-PCR.
Effects of Acetyl-Coenzyme A Carboxylase Inhibitors on Root Cell Transmembrane Electric Potentials in Graminicide-Tolerant and -Susceptible Corn (Zea mays L.).
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Herbicidal activity of aryloxyphenoxypropionate and cyclohexanedione herbicides (graminicides) has been proposed to involve two mechanisms: inhibition of acetyl-coenzyme A carboxylase (ACCase) and depolarization of cell membrane potential. We examined the effect of aryloxyphenoxypropionates
Susceptibilities of Different Test Systems from Maize (Zea mays), Poa annua, and Festuca rubra to Herbicides That Inhibit the Enzyme Acetyl-Coenzyme A Carboxylase
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The susceptibilities of maize (Zea mays cv. Champ) and two graminicide-resistant grass species, Poa annua (annual meadow grass) and Festuca rubra (red fescue), to two aryloxyphenoxypropionates (quizalofop and fluazifop) and a cyclohexanedione (sethoxydim) graminicide were evaluated in leaf blades
Partial purification and biochemical characterization of a heteromeric protein phosphatase 2A holoenzyme from maize (Zea mays L.) leaves that dephosphorylates C4 phosophoenolpyruvate carboxylase.
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The activity and allosteric properties of plant phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) are controlled posttranslationally by specific reversible phosphorylation of a strictly conserved serine residue near the N-terminus. This up/down-regulation of PEPC is catalyzed by a dedicated and
Re-examination of the roles of PEP and Mg2+ in the reaction catalysed by the phosphorylated and non-phosphorylated forms of phosphoenolpyruvate carboxylase from leaves of Zea mays. Effects of the activators glucose 6-phosphate and glycine.
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To study the effects of phosphoenolpyruvate (PEP) and Mg2+ on the activity of the non-phosphorylated and phosphorylated forms of phosphoenolpyruvate carboxylase (PEPC) from Zea mays leaves, steady-state measurements have been carried out with the free forms of PEP (fPEP) and Mg2+ (fMg2+), both in a
Expression of the Acc1 Gene-Encoded Acetyl-Coenzyme A Carboxylase in Developing Maize (Zea mays L.) Kernels.
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A mutation (Acc1-S2) in the structural gene for maize (Zea mays L.) acetyl-coenzyme A carboxylase (ACCase) that significantly reduces sethoxydim inhibition of leaf ACCase activity was used to investigate the gene-enzyme relationship regulating ACCase activity during oil deposition in developing
Metal Ion Interactions with Phosphoenolpyruvate Carboxylase from Crassula argentea and Zea mays.
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Metal ion interactions with phosphoenolpyruvate carboxylase from the CAM plant Crassula argentea and the C(4) plant Zea mays were kinetically analyzed. Fe(2+) and Cd(2+) were found to be active metal cofactors along with the previously known active metals Mg(2+), Mn(2+), and Co(2+). In studies with
Kinetics of phosphoenolpyruvate carboxylase from Zea mays leaves at high concentration of substrates.
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At low concentrations of phosphoenolpyruvate and magnesium, the substrate of phosphoenolpyruvate carboxylase (PEPC) from Zea mays leaves is the MgPEP complex and free phosphoenolpyruvate (fPEP) is an allosteric activator [A. Tovar-Méndez, R. Rodríguez-Sotres, D.M. López-Valentín, R.A. Muñoz-Clares,
Mechanistic studies of phosphoenolpyruvate carboxylase from Zea mays with (Z)- and (E)-3-fluorophosphoenolpyruvate as substrates.
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The catalytic mechanism of phosphoenolpyruvate (PEP) carboxylase from Zea mays has been studied using (Z)- and (E)-3-fluorophosphoenolpyruvate (F-PEP) as substrates. Both (Z)- and (E)-F-PEP partition between carboxylation to produce 3-fluorooxalacetate and hydrolysis to produce 3-fluoropyruvate.
Influence of allosteric effectors on the kinetics and equilibrium binding of phosphoenolpyruvate (PEP) to phosphoenolpyruvate carboxylase (PEPC) from Zea mays.
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Phosphoenolpyruvate carboxylase (PEPC) the carbon dioxide processing enzyme of C(4) plants, shows the features of an allosteric enzyme. Allosteric activators such as D-glucose-6-phosphate and glycine increase the affinity of PEPC for its substrate PEP at pH 8.0 and pH 7.0. Allosteric inhibitors like
A kinetic investigation of phosphoenolpyruvate carboxylase from Zea mays.
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The reaction catalyzed by phosphoenolpyruvate carboxylase from Zea mays has been studied kinetically. Results of initial velocity patterns and inhibition studies indicate that phosphoenolpyruvate carboxylase has a random sequential mechanism in which there is a high level of synergism in the binding
Effects of dietary corn oil and vitamin E supplementation on fatty acid profiles and expression of acetyl CoA carboxylase and stearoyl-CoA desaturase gene in Hu sheep.
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This study was conducted to assess the effects of dietary corn oil and vitamin E supplementation on fatty acid (FA) profiles and abundances of acetyl-CoA carboxylase (ACC) and Delta(9) stearoyl-CoA desaturase (SCD) mRNA of Hu sheep. Animals were allocated to three dietary treatments: basal and
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