FosfoenolPiruvato. AH Universidad del mar. La enzima fosfoenolpiruvato carboxilasa. Fecha de consulta: 13/Noviembre/ Consultado. En este trabajo, investigamos la compleja regulación alostérica de la formas no fosforiladas de las isoenzimas fotosintéticas de la fosfoenolpiruvato carboxilasa. Acetil-CoA = acetil-coenzima A, MDH = malato deshidrogenasa, OAA = oxalacetato, PEP = fosfoenolpiruvato, PEPC = fosfoenolpiruvato carboxilasa piruvato y.

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Received February 23, Accepted June 8, In leaves of C4 plants the initial reaction in the assimilation pathway of atmospheric Fosfoenolpuruvato 2 is the essentially irreversible carboxylation of phospho eno lpyruvate PEP by phospho eno lpyruvate carboxylase orthophosphate: But they are by no means redundant. The concentration of phosphorylated sugars increases when the Calvin cycle is active.

Neutral amino acids concentrations, particularly that of Gly, increase under photorespiration conditions [15]. Therefore, the two kinds of activators act as metabolic signals that indicate the necessity of increasing the flux through the C4 cycle, in order to keep pace with the flux rate of the Calvin cycle in the case of Glc6P, or to increase the supply of CO 2 to the bundle sheath cells to prevent photorespiration, in the case of Gly.

While Glc6P is unable to revert the inhibition caused by a physiological concentration of malate, Gly can produce an enzyme almost as active than that in the absence of the foosfoenolpiruvato [14].

The kinetic differences between the allosteric activators acquire special relevance under conditions close to those prevailing under illumination, i. Activation by Glc6P could be rosfoenolpiruvato during the night or at the onset of illumination before the buildup of malate that takes place during the first hour cwrboxilasa illumination [16]. Once the levels of malate are high, saturation of the Glc6P allosteric site would give only a marginal advantage.

Photorespiration surely follows the buildup of malate during the day because of a decrease of the C4 cycle flux, a decrease due to both PEPC inhibition by the increased malate concentration and depletion of the available CO 2 fosfoenolpkruvato a very active Calvin cycle. Activation by Gly helps in increasing the flux through the C4 pathway by effectively counteracting the inhibitory effects of malate, and, therefore, it helps in increasing the concentrations of CO2 in the bundle sheet cells thus overcoming photorespiration.

The bicarbonate concentration in an assay medium in contact with air at pH 7. Also, because regulation of PEPC activity by metabolite effectors is mostly exerted at subsaturating concentrations of substrate [21], in the studies with the allosteric effectors we used a carboxklasa total PEP tPEP concentration of only 0.

The results of these kinetic experiments are shown in Figure 1 and summarized in dable 1. These two limiting concentrations of tPEP are close to those existing in the cytosol of the mesophyll cells during the dark and light periods, respectively [22, 23]. Glc6P binds cooperatively to both enzymes, with h values close to 2. The activation by Glc6P may, however, play an important role increasing the flux of the C4 cycle at the onset of the light conditions, as mentioned above.

The differences between the two enzymes in the degree of cooperativity in the binding of PEP in the presence of a high malate fksfoenolpiruvato are in full agreement with their differences in malate affinity. Although the S 0. carboxiilasa


Term Bank – carboxilasa – Spanish English Dictionary

When near physiological concentrations were used, Glc6P was very ineffective in overcoming malate inhibition [14]. Gly has been found to be much more effective than Glc6P in this respect under conditions close to those existing in vivo during the light period [14]. We tested now the relative contribution of the two kinds of activators in relieving malate inhibition of the two C4 isoenzymes at the tPEP concentration existing during the night, 0.

These results indicate that the binding of malate and that of Glc6P to the amaranth enzyme are competitive. These catboxilasa suggest that the binding of Glc6P is not affected by the binding of the inhibitor to this enzyme. This is consistent with a lack of effect of malate on the binding of Glc6P and, reciprocally, a lack of effect of Glc6P on the binding of malate. Therefore, under our experimental conditions Glc6P is no carboxilaaa effective in counteracting malate inhibition of the amaranth than of the maize enzyme Fig.

This is consistent with competition between inhibitor and activator for their binding to the enzyme. These results show that Gly is not an activator of the dicot enzyme either in the absence or in the presence of the inhibitor malate.

Six of these sequences are from monocot plants and the other crboxilasa from dicot plants. The overall identity among monocot isoenzymes ranged from 80 to ffosfoenolpiruvato In this loop there are several amino acid residues that are conserved, or with conservative substitutions, within each group of monocots or dicots enzymes, but that differ from one carboxilaxa to the other marked with an asterisk in Figure 3.


The neutral amino acid binding site is not yet known because no structure with this kind of ligand has been determined so far. In the homology models of both enzymes, these parts are forming loops, as expected. Of particular interest to fosfoenolpuruvato is the loop analyzed in the sequence alignments of Figure 3. A rigid docking of glycine in this position not shown suggested the feasibility of binding of the activator to these residues, as we propose.

As a consequence of this, D and K in the maize enzyme model are not crboxilasa well positioned to bind the activator molecule as they are in the amaranth enzyme model, as indicated by a rigid docking of the Gly molecule in this site not shownwhich is consistent with the A 0.

The allosteric transition would not occur in the amaranth enzyme, thus accounting for the huge differences between the amaranth and the maize enzymes in their degree of activation achieved at saturation by Gly.

Both types of isoenzymes also differ in their affinity for the substrate PEP, the activator Glc6P and the inhibitor malate. The lack of activation by Gly of the dicot isoenzymes is mainly compensated by their higher affinity for the substrate PEP and their lower affinity for the inhibitor malate than those exhibited by the monocot isoenzymes.

EDTA ethylenediaminetetraacetic acid disodium salt was from Merck. All other chemicals carboxilasq analytical grade were fosfoenolpiruvsto standard suppliers. Plants of maize Zea mays L.


Fully expanded leaves were used for the experiments. Amaranth Amaranthus hypochondriacus L. Phosphoenolpyruvate carboxylase extraction, purification and assay. Plants were kept in darkness for at least 6 h ccarboxilasa to extraction.

Protein was measured by the method of Bradford [33], using bovine serum albumin as the standard. Phosphoenolpyruvate carboxylase fosfoenolplruvato and kinetic studies. The standard assay medium, final volume of 0. The reaction was started by addition of the enzyme preparation. Rates in the absence of PEP were negligible.

Each determination was performed at least in duplicate. One farboxilasa of PEPC is defined as the amount of enzyme needed to catalyze the formation of 1 umol of oxalacetate per min under our experimental conditions.

No exogenous bicarbonate was added to the assay media, so that the concentration of bicarbonate was 0. We display the results of the kinetics of saturation of the enzyme by its substrate PEP by considering carboxilaasa as the variable substrate, instead of MgPEP, to facilitate the evaluation of the data in the physiological range of concentration of this metabolite.

Malate concentrations ranged from 0 to 20 mM; Glc6P concentrations from 0 to 20 mM; and Gly concentrations from 0 to mM in the absence of malate, or from 0 to mM in the presence of this inhibitor. Kinetic data were analyzed by nonlinear regression calculations using a commercial computing program formulated with the algorithm of Marquardt [35].

Initial velocity data depending upon varied concentration of substrate were fitted to a Hill equation equation 1: In the experiments in which the concentration of the activator was varied at constant concentration of substrates, equation 2 was used: When the concentration of inhibitor was varied at constant concentration of substrates, the experimental data were fitted carboxiasa equation 3: The points in the figures are the experimentally determined values, whereas the curves are calculated from fits of these data to the appropriate equation.

The best fits were determined by the relative fit error, error of the constants and absence of significant correlation between the residuals, and other relevant variables like observed velocities, substrate concentration and data number.

FosfoenolPiruvato by Ariadne Heredia on Prezi

Sequence carboxilasx and homology model building. Progressive multiple sequence alignment was carried out with the ClustalX package [38], using penalties based on secondary structure.

The same solution was always obtained after repeated submissions of the data to this server. The models were validated using ProCheck [40]. The figure was created with PyMOL [41].

Nishikido, T; Takanashi, H. Nature, Introduction In leaves of C4 plants the initial reaction in the assimilation pathway of atmospheric CO 2 is the essentially irreversible carboxylation of phospho eno lpyruvate PEP by phospho eno lpyruvate carboxylase orthophosphate: Plant material Plants of maize Zea mays L.

Phosphoenolpyruvate carboxylase extraction, purification and assay Plants were kept in darkness for at least 6 h prior to extraction. Data analysis Kinetic data were analyzed by nonlinear regression calculations using a commercial computing program formulated with the algorithm of Marquardt [35].

Barranca del Muerto Fosfoenolpiruvsto.