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Query: EC:4.1.1.32 (phosphoenolpyruvate carboxykinase)
 4,204 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Plasma membrane (PM) H(+)-ATPase and H(+) transport activity were detected in PM fractions prepared from Zostera marina (a seagrass), Vallisneria gigantea (a freshwater grass) and Oryza sativa (rice, a terrestrial plant). The properties of Z. marina PM H(+)-ATPase, specifically, the optimal pH for ATPase activity and the result of trypsin treatment, were similar to those of authentic PM H(+)-ATPases in higher plants. In V. gigantea and O. sativa PM fractions, vanadate-sensitive (P-type) ATPase activities were inhibited by the addition of NaCl. In contrast, activity in the Z. marina PM fraction was not inhibited. The nitrate-sensitive (V-type) and azide-sensitive (F-type) ATPase activities in the Z. marina crude microsomal fraction and the cytoplasmic phosphoenolpyruvate carboxylase activity, however, were inhibited by NaCl, indicating that not all enzyme activities in Z. marina are insensitive to salt. Although the ratio of Na(+) to K(+) (Na(+)/K(+)) in seawater is about 30, Na(+)/K(+) in the Z. marina cells was about 1.0. The salt-tolerant ATPase activity in the plasma membrane must play an important role in maintaining a low Na(+) concentration in the seagrass cells.
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PMID:Salt-tolerant ATPase activity in the plasma membrane of the marine angiosperm Zostera marina L. 1240 93

C(4) phosphoenolpyruvate carboxylase (PEPCase: EC 4.1.1.31) is subjected to in vivo regulatory phosphorylation by a light up-regulated, calcium-independent protein kinase. Salt stress greatly enhanced phosphoenolpyruvate carboxylase-kinase (PEPCase-k) activity in leaves of Sorghum. The increase in PEPCase-k anticipated the time course of proline accumulation thereby suggesting that water stress was not involved in the kinase response to salt. Moreover, osmotic stress seemed not to be the main factor implicated, as demonstrated by the lack of effect when water availability was restricted by mannitol. In contrast, LiCl (at a concentration of 10 mM in short-term treatment of both excised leaves and whole plants) mimicked the effects of 172 mM NaCl salt-acclimation, indicating that the rise in PEPCase-k activity resulted primarily from the ionic stress. Both NaCl and LiCl treatments increased the activity of a Ca(2+)-independent, 35 kDa kinase, as demonstrated by an in-gel phosphorylation experiment. Short-term treatment of excised leaves with NaCl or LiCl partially reproduces the effects of whole plant treatments. Finally, salinization also increased PEPCase-k activity and the phosphorylation state of PEPCase in darkened Sorghum leaves. This fact, together with increased malate production during the dark period, suggests a shift towards mixed C(4) and crassulacean acid metabolism types of photosynthesis in response to salt stress.
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PMID:Characterization of salt stress-enhanced phosphoenolpyruvate carboxylase kinase activity in leaves of Sorghum vulgare: independence from osmotic stress, involvement of ion toxicity and significance of dark phosphorylation. 1256 7

Two novel phosphoenolpyruvate carboxylase (PEPC) isoforms have been biochemically characterized from endosperm of developing castor oil seeds (COS). The association of a 107 kDa PEPC subunit (p107) with an immunologically unrelated bacterial PEPC-type 64 kDa polypeptide leads to marked physical and kinetic differences between the PEPC1 p107 homotetramer and PEPC2 p107/p64 heterooctamer. COS p107 is quite susceptible to limited proteolysis during PEPC purification. An endogenous asparaginyl endopeptidase appears to catalyze the in vitro cleavage of an approximately 120 amino acid polypeptide from the N-terminal end of p107, producing a truncated 98 kDa polypeptide (p98). Immunoblotting was used to estimate proteolytic activity by following the disappearance of p107 and concomitant appearance of p98 during incubation of clarified COS extracts at 4 degrees C. The in vitro proteolysis of p107 to p98 only occurred in the combined presence of 2 mM dithiothreitol and high salt concentrations (particularly SO(4) (2-) and PO(4) (2-) salts). Although p107-degrading activity was present throughout COS development, it was most pronounced in endosperm extracts from older beans. Several protease inhibitors, including two commercially available protease inhibitor cocktails, were tested for their ability to prevent p107 proteolysis. All of the inhibitors were ineffective except for 2,2'-dipyridyl disulfide (DPDS), a relatively inexpensive and underutilized active site inhibitor of plant thiol proteases. Asparaginyl endopeptidase activity of COS extracts was unaffected by 20% (NH(4))(2)SO(4) when determined in the presence or absence of 2 mM dithiothreitol using a spectrophotometric assay based upon the hydrolysis of benzoyl-L-Asn-p-nitroanilide. Thus, we propose that the combined presence of 2 mM dithiothreitol and 20% (NH(4))(2)SO(4) promotes a p107 conformational change that exposes the N-terminal region asparaginyl residue where p107 hydrolysis is believed to occur.
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PMID:In vitro proteolysis of phosphoenolpyruvate carboxylase from developing castor oil seeds by an endogenous thiol endopeptidase. 1618 75

The phosphoenolpyruvate carboxylase (PEPC) gene family of Arabidopsis is composed of four genes. Based on sequence analysis it was deduced that Atppc1, Atppc2 and Atppc3 genes encode plant-type PEPCs, whereas Atppc4 encodes a PEPC without phosphorylation motif, but no data at the protein level have been reported. Here, we describe the analysis of the four Arabidopsis PEPC polypeptides, which were expressed in Escherichia coli. Immunological characterization with anti plant-type PEPC and an anti-AtPPC4 antibody, raised in this work, showed that the bacterial-type PEPC is unrelated with plant-type PEPCs. Western-blot analysis of different Arabidopsis organs probed with anti plant-type PEPC antibodies detected a double band, the one with low molecular weight corresponding to the three plant-type PEPCs. The high molecular weight subunit is not encoded by any of the Arabidopsis PEPC genes. No bands were detected with the anti-AtPPC4 antibody. PEPC genes show differential expression in Arabidopsis organs and in response to environmental stress. Atppc2 transcripts were found in all Arabidopsis organs suggesting that it is a housekeeping gene. In contrast, Atppc3 gene was expressed in roots and Atppc1 in roots and flowers, as Atppc4. Highest PEPC activity was found in roots, which showed expression of the four PEPC genes. Salt and drought exerted a differential induction of PEPC gene expression in roots, Atppc4 showing the highest induction in response to both stresses. These results show that PEPC is part of the adaptation of the plant to salt and drought and suggest that this is the function of the new bacterial-type PEPC.
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PMID:Arabidopsis phosphoenolpyruvate carboxylase genes encode immunologically unrelated polypeptides and are differentially expressed in response to drought and salt stress. 1628 77

Under salt stress conditions, the level of CpNpG-methylation (N is any nucleoside) of the nuclear genome of the facultative halophyte Mesembryanthemum crystallinum in the CCWGG sequences (W = A or T) increases two-fold and is coupled with hypermethylation of satellite DNA on switching-over of C3-photosynthesis to the crassulacean acid metabolism (CAM) pathway of carbon dioxide assimilation. The methylation pattern of the CCWGG sequences is not changed in both the 5'-promoter region of the gene of phosphoenolpyruvate carboxylase, the key enzyme of C4-photosynthesis and CAM, and in the nuclear ribosomal DNA. Thus, a specific CpNpG-hypermethylation of satellite DNA has been found under conditions of expression of a new metabolic program. The functional role of the CpNpG-hypermethylation of satellite DNA is probably associated with formation of a specialized chromatin structure simultaneously regulating expression of a large number of genes in the cells of M. crystallinum plants on their adaptation to salt stress and switching-over to CAM metabolism.
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PMID:Effect of hypermethylation of CCWGG sequences in DNA of Mesembryanthemum crystallinum plants on their adaptation to salt stress. 1661 68

In Mesembryanthemum crystallinum, salt stress induces the accumulation of proline and a specific isoform of the enzyme phosphoenolpyruvate carboxylase (PEPCase) prior to the switch from C(3) to Crassulacean acid metabolism (CAM). To determine whether plant growth regulators initiate or imitate these responses, we have compared the effects elicited by NaCl, abscisic acid (ABA), and cytokinins using PEPCase and proline levels as diagnostic tools. Exogenously applied ABA is a poor substitute for NaCl in inducing proline and CAM-specific PEPCase accumulation. Even though ABA levels increase 8- to 10-fold in leaves during salt stress, inhibition of ABA accumulation does not affect these salt-induced responses. In contrast, the addition of cytokinins (6-benzylaminopurine, zeatin, 2-isopentyladenine) mimic salt by greatly increasing proline and PEPCase amounts. Endogenous zeatin levels remain unchanged during salt stress. We conclude: (a) The salt-induced accumulation of proline and PEPCase is coincident with, but is not attributable to, the rise in ABA or zeatin concentration. (b) For the first time, cytokinins and NaCl are implicated as independent initiators of a sensing pathway that signals leaves to alter PEPCase gene expression. (c) During stress, the sensing of osmotic imbalances leading to ABA, proline, and CAM-specific PEPCase accumulation may be mediated directly by NaCl.
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PMID:Convergent Induction of Osmotic Stress-Responses : Abscisic Acid, Cytokinin, and the Effects of NaCl. 1665 78

Excised roots of barley (Hordeum vulgare, var. Campana) lost organic acids, amino acids, K(+), and Cl(-) within 15 minutes after initiation of anaerobic treatment or treatment with NaCN and 2,4-dinitrophenol. Initial loss of organic acids when roots were placed under N(2) is attributed to a decarboxylation reaction, possibly catalyzed by phosphoenolpyruvate carboxykinase. Organic and amino acids began to leak from the roots to the bathing medium after 1 to 2 hours under N(2), indicating injury to cell membranes. During the first hour of anaerobic treatment, K(+) loss from low-salt roots was equivalent to organic acid loss. Potassium loss from roots containing high levels of KCl was approximately equal to organic acid plus amino acid loss; and Cl(-) loss was approximately equal to amino acid loss. It is postulated that, within cells, organic acids may electrostatically bind an equivalent quantity of cations and that amino acids may bind an equivalent quantity of both cations and anions.
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PMID:Loss of organic acids, amino acids, k, and cl from barley roots treated anaerobically and with metabolic inhibitors. 1665 12

The relationship of malate synthesis to K(+) absorption from solutions of K(2)SO(4) and KHCO(3) was compared in nonvacuolate barley (Hordeum vulgare) root tips and whole excised roots. The comparison has permitted separation of the process which evokes organic acid synthesis from that which leads to stoichiometry between net acid equivalents formed and excess K(+) absorbed from K(2)SO(4), on the one hand, and total K(+) absorbed from KHCO(3), on the other. Both in tips and in roots K(+) uptake from 20 mN salt solution exceeds malate synthesis in the first hour. In vacuolate roots the expected stoichiometry is achieved with time. When root tips are transferred to dilute CaSO(4), malate is rapidly metabolized, and K(+) is lost to the solution. By contrast, in excised whole roots the malate level remains unchanged, the salt-induced organic acid presumably being retained in the vacuole. In excised roots malonate leads to a marked drop in malate levels in untreated roots as well as in roots which have experienced salt-induced net malate synthesis. In consequence, it is contended that malonate makes available normally sequestered vacuolar malate.The general hypothesis is offered that the bicarbonate level of the cytoplasm controls organic acid synthesis by phosphoenolpyruvate carboxylase, and that the cytoplasmic bicarbonate level is raised either by exchange of cytoplasmic H(+) for external cation, or by bicarbonate absorption directly. Stoichiometry, in turn, is achieved by the accumulation in the vacuole of the double salt of malate.
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PMID:Bicarbonate Fixation and Malate Compartmentation in Relation to Salt-induced Stoichiometric Synthesis of Organic Acid. 1665 54

This paper reports effects of salts on in vitro activity of phosphoenolpyruvate carboxylase and ribulose-1,5-diphosphate carboxylase, isolated from species differing in salt tolerance.Inhibition of phosphoenolpyruvate carboxylase by the inorganic salts KCl, NaCl, and Na(4)SO(4) depended on the source of the enzyme. Phosphoenolpyruvate carboxylase isolated from leaves of C(4) plants was extremely sensitive to inorganic salts, whereas the enzyme extracted from roots of C(4) plants or from both shoots and roots of C(3) plants was much less sensitive. Ribulose-1,5-diphosphate carboxylase was less salt-sensitive than the phosphoenolpyruvate carboxylases. Differences in salt sensitivity of carboxylases were observed over a wide pH range. The results suggest substantial physical-chemical differences between phosphoenolpyruvate carboxylases functioning in photosynthesis and in CO(2) dark fixation.Among C(4) species, phosphoenolpyruvate carboxylase from halophytic species was more salt-sensitive than that from a salt-sensitive species. This anomaly, between in vitro response of enzymes and growth response of the plants, is briefly discussed.
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PMID:Salt responses of carboxylation enzymes from species differing in salt tolerance. 1665 37

Malate synthesis by CO(2) fixation in wheat (Triticum aestivum L.) and lupin (Lupinus luteus) roots was investigated by labeling with NaH(13)CO(3) as well as with NaH(14)CO(3). The distribution of (14)C label in the malate was examined, using enzymic degradation methods (malic enzyme, pyruvate decarboxylase) and, in the case of (13)C, gas chromatography-mass spectrometry. In long-term experiments (2 to 12 hours), both methods showed that the [1-C] and [4-C] positions of malic acid are approximately equally labeled, in agreement with former findings. Short-term experiments (15, 30 seconds) showed that (14)C is confined initially to the [4-C] position of malate but then is distributed quickly to the [1-C] atom. Neither labeling pattern nor rate of randomization was influenced by salt treatment. Analysis of malate from roots by gas chromatography-mass spectrometry, a procedure which was tested against in vitro-prepared [1-(13)C]-, [4-(13)C]-, and [1,4-(13)C] malate, gave strong evidence for the existence of only singly labeled malate molecules. These data suggest that only one carboxylation step, catalyzed by phosphoenolpyruvate carboxylase and/or phosphoenolpyruvate carboxykinase, is responsible for malic acid synthesis in roots and that malate label is randomized by a fumarase-like reaction, presumably in mitochondria.
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PMID:Pathway of malic Acid synthesis in response to ion uptake in wheat and lupin roots: evidence from fixation of C and C. 1666 88


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