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Query: EC:4.1.1.49 (
phosphoenolpyruvate carboxykinase
)
4,654
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The intracellular locations of six key enzymes of Crassulacean acid metabolism were determined using enzymically isolated mesophyll protoplasts of Sedum praealtum D.C. Data from isopycnic sucrose density gradient centrifugation established the chloroplastic location of pyruvate Pi dikinase, the mitochondrial location of
NAD
-linked malic enzyme, and exclusively nonparticulate (not associated with chloroplasts, peroxisomes, or mitochondria) locations of
phosphoenolpyruvate carboxylase
, NADP-linked malic enzyme, enolase, and phosphoglycerate mutase. The consequences of this enzyme distribution with respect to compartmentalization of the pathway and the transport of metabolites in Crassulacean acid metabolism are discussed.
...
PMID:Intracellular Localization of Some Key Enzymes of Crassulacean Acid Metabolism in Sedum praealtum. 1666 Aug 3
Suaeda monoica Frossk. ex J. F. Gmel is a C(4) plant with three different photosynthesizing cell layers. The outer chlorenchymatous layer shows a high activity of phosphoenolpyruvate (PEP) carboxylase but none of ribulose bisphosphate (RuBP) carboxylase. The electrophoretic protein band of RuBP carboxylase was missing in this layer. The second chlorenchymatous cells layer shows a very high activity of RuBP carboxylase and
NAD
malic enzyme and only traces of activity of
PEP carboxylase
. The third photosynthesizing cell type is comprised of the water tissue. It has moderate activities of RuBP carboxylase and
PEP carboxylase
. A model for carbon flow in Suaeda monoica leaves is proposed.
...
PMID:Biochemical Specialization of Photosynthetic Cell Layers and Carbon Flow Paths in Suaeda monoica. 1666 Nov 14
The CO(2) compensation point of the submersed aquatic macrophyte Hydrilla verticillata varied from high (above 50 microliters per liter) to low (10 to 25 microliters per liter) values, depending on the growth conditions. Plants from the lake in winter or after incubation in an 11 C/9-hour photoperiod had high values, whereas summer plants or those incubated in a 27 C/14-hour photoperiod had low values. The plants with low CO(2) compensation points exhibited dark (14)CO(2) fixation rates that were up to 30% of the light fixation rates. This fixation reduced respiratory CO(2) loss, but did not result in a net uptake of CO(2) at night. The low compensation point plants also showed diurnal fluctuations in titratable acid, such as occur in Crassulacean acid metabolism plants. However, dark fixation and diurnal acid fluctuations were negligible in Hydrilla plants with high CO(2) compensation points.Exposure of the low compensation point plants to 20 micromolar (14)CO(2) resulted in 60% of the (14)C being incorporated into malate and aspartate, with only 16% in sugar phosphates. At a high CO(2) level, the C(4) acid label was decreased. A pulse-chase study indicated that the (14)C in malate, but not aspartate, decreased after a long (270-second) chase period; thus, the C(4) acid turnover was much slower than in C(4) plants.Phosphoenolpyruvate carboxylase activity was high (330 micromoles per milligram chlorophyll per hour), as compared to ribulose bisphosphate carboxylase (20 to 25), in the plants with low compensation points. These plants also had a pyruvate, Pi dikinase activity in the leaves of 41 micromoles per milligram chlorophyll per hour, which suggests they are not C(3) plants.
NAD
- and NADP(+)-malate dehydrogenase activities were 6136 and 24.5 micromoles per milligram chlorophyll per hour, respectively. Of the three decarboxylating enzymes assayed, the activities of
NAD
- and NADP(+)-malic enzyme were 104.2 and 23.7 micromoles per milligram chlorophyll per hour, while
phosphoenolpyruvate carboxykinase
was only 0.2.Low compensation point Hydrilla plants fix some CO(2) into C(4) acids, which can be decarboxylated for later refixation, presumably into the Calvin cycle. Refixation would be advantageous in summer lake environments where the CO(2) levels are high at night but low during the day. Hydrilla does not fit any of the present photosynthetic categories, and may have to be placed into a new group, together with other submersed aquatic macrophytes that have environmentally variable CO(2) compensation points.
...
PMID:C(4) Acid Metabolism and Dark CO(2) Fixation in a Submersed Aquatic Macrophyte (Hydrilla verticillata). 1666 Nov 84
Incubation under water in a 30 C/14-hour or 12 C/10-hour photoperiod caused the CO(2) compensation points of 10 aquatic macrophytes to decrease below 25 or increase above 50 microliters CO(2) per liter, respectively. Submerged and aerial leaves of two amphibious angiosperms (Myriophyllum brasiliense and Proserpinaca palustris) maintained high compensation points when incubated in air but, when the submerged or aerial leaves of Proserpinaca were incubated under water, the compensation points dropped as low as 10. This suggests that, in addition to temperature and photoperiod, some factor associated with submergence regulates the compensation point of aquatic plants. In the high-compensation point plants, photorespiration, as a percentage of net photosynthesis, was equivalent to that in terrestrial C(3) plants. For Hydrilla verticillata, the decreasing CO(2) compensation points (110, 40, and 10) were associated with reduced photorespiration, as indicated by decreased O(2) inhibition, decreased rates of CO(2) evolution into CO(2)-free air, and increased net photosynthetic rates.The decrease in the CO(2) compensation points of Hydrilla, Egeria densa, and Cabomba caroliniana was accompanied by an increase in the activity of phosphoenolpyruvate, but not of ribulose bisphosphate, carboxylase. In Hydrilla, several C(4) enzymes also increased in activity to the following levels (micromoles per gram fresh weight per hour): pyruvate Pi dikinase (35), pyrophosphatase (716), adenylate kinase (525),
NAD
and NADP malate dehydrogenase (6565 and 30),
NAD
and NADP malic enzymes (239 and 44), and aspartate and alanine aminotransferases (357 and 85), whereas glycolate oxidase (6) and phosphoglycolate and phosphoglycerate phosphatases (76 and 32) showed no change. Glycolate dehydrogenase and
phosphoenolpyruvate carboxykinase
were undetectable. The reduced photorespiration in these plants may be due to increased CO(2) fixation via a C(4) acid pathway. However, for three Myriophyllum species, some other mechanism appears operative, as
phosphoenolpyruvate carboxylase
was not increased in the low compensation point state, and ribulose bisphosphate carboxylase remained the predominant carboxylation enzyme.
...
PMID:Induction of reduced photorespiratory activity in submersed and amphibious aquatic macrophytes. 1666 70
The succulent, cylindrical leaves of the C(4) dicot Portulaca grandiflora possess three distinct green cell types: bundle sheath cells (BSC) in radial arrangement around the vascular bundles; mesophyll cells (MC) in an outer layer adjacent to the BSC; and water storage cells (WSC) in the leaf center. Unlike typical Kranz leaf anatomy, the MC do not surround the bundle sheath tissue but occur only in the area between the bundle sheath and the epidermis. Intercellular localization of photosynthetic enzymes was characterized using protoplasts isolated enzymatically from all three green cell types.Like other C(4) plants, P. grandiflora has ribulose 1,5-bisphosphate carboxylase and the decarboxylating enzyme, NADP(+)-malic enzyme, in the BSC. Unlike other C(4) plants, however,
phosphoenolpyruvate carboxylase
, pyruvate, Pi dikinase, and NADP(+)-malate dehydrogenase of the C(4) pathway were present in all three green cell types, indicating that all are capable of fixing CO(2) via
phosphoenolpyruvate carboxylase
and regenerating phosphoenolpyruvate. Other enzymes were about equally distributed between MC and BSC similar to other C(4) plants. The enzyme profile of the WSC was similar to that of the MC but with reduced activity in most enzymes, except mitochondrion-associated enzymes.Intracellular localization of enzymes was studied in organelles partitioned by differential centrifugation using mechanically ruptured mesophyll and bundle sheath protoplasts. Phosphoenolpyruvate carboxylase was a cytosolic enzyme in both cells; whereas, ribulose 1,5-bisphosphate carboxylase and NADP(+)-malic enzyme were exclusively compartmentalized in the bundle sheath chloroplasts. NADP(+)-malate dehydrogenase, pyruvate, Pi dikinase, aspartate aminotransferase, 3-phosphoglycerate kinase, and NADP(+)-triose-P dehydrogenase were predominantly localized in the chloroplasts while alanine aminotransferase and
NAD
(+)-malate dehydrogenase were mainly present in the cytosol of both cell types. Based on enzyme localization, a scheme of C(4) photosynthesis in P. grandiflora is proposed.Well-watered plants of P. grandiflora exhibit a diurnal fluctuation of total titratable acidity, with an amplitude of 61 and 54 microequivalent per gram fresh weight for the leaves and stems, respectively. These changes were in parallel with changes in malic acid concentration in these tissues. Under severe drought conditions, diurnal changes in both titratable acidity and malic acid concentration in both leaves and stems were much reduced. However, another C(4) dicot Amaranthus graecizans (nonsucculent) did not show any diurnal acid fluctuation under the same conditions. These results confirm the suggestion made by Koch and Kennedy (Plant Physiol. 65: 193-197, 1980) that succulent C(4) dicots can exhibit an acid metabolism similar to Crassulacean acid metabolism plants in certain environments.
...
PMID:Photosynthetic Characteristics of Portulaca grandiflora, a Succulent C(4) Dicot : CELLULAR COMPARTMENTATION OF ENZYMES AND ACID METABOLISM. 1666 54
Mesembryanthemum crystallinum, a halophilic, inducible Crassulacean acid metabolism (CAM) species, was grown at NaCl concentrations of 20 and 400 millimolar in the rooting medium. Plants from the low salinity treatment showed exclusively C(3)-photosynthetic net CO(2) fixation, whereas plants exposed to the high salinity level exhibited net CO(2) dark fixation involving CAM. Mesophyll protoplasts, isolated from both tissues, were gently ruptured, and the intracellular localization of enzymes was studied following differential centrifugation and Percoll density gradient centrifugation of protoplast extracts. Both centrifugation techniques resulted in the separation of intact chloroplasts, with up to 90% yield, from other organelles and the nonparticulate fraction of cells. Enzymes were identified by determination of activity and by sodium dodecyl sulfate gel electrophoresis of enzyme protein.Experiments established the extraorganellar (cytoplasmic) location of
phosphoenolpyruvate carboxylase
, enolase, phosphoglyceromutase, and NADP-malic enzyme; the mitochondrial location of NAD-malic enzyme; and the chloroplastic location of pyruvate, Pi dikinase.
NAD
-glyceraldehyde-3-phosphate dehydrogenase, phosphohexose isomerase, and phosphoglycerate kinase were associated with both cytoplasm and chloroplasts. NADP-dependent malate dehydrogenase activity was found in both the chloroplastic and extrachloroplastic fractions; the activity in the chloroplast showed an optimum at pH 8.0 and was dependent upon preincubation of enzyme with dithiothreitol. The extrachloroplastic activity showed an optimum at pH 6.5 and was independent of pretreatment with dithiothreitol. Protoplast extracts of M. crystallinum performing CAM exhibited higher activities (expressed per mg chlorophyll per min) of
phosphoenolpyruvate carboxylase
, pyruvate, Pi dikinase, NADP-malic enzyme, NAD-malic enzyme, NADP-malate dehydrogenase, enolase, phosphoglyceromutase,
NAD
-glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, and phosphohexose isomerase than protoplast extracts from M. crystallinum not exhibiting CAM. The increase in total activity of the latter three enzymes following exposure of plants to 400 millimolar NaCl and the development of CAM was due to specific increases in the levels of activity in the cytoplasm.
...
PMID:Intracellular Localization of Enzymes of Carbon Metabolism in Mesembryanthemum crystallinum Exhibiting C(3) Photosynthetic Characteristics or Performing Crassulacean Acid Metabolism. 1666 97
Pea (Pisum sativum L. cv ;Little Marvel') plants were exposed to SO(2) for short term (3 hours) and long term (2 days) at 0.2 and at 0.5 microliter per liter (ppm) levels. The effect of this treatment on the activity of
phosphoenolpyruvate carboxylase
,
NAD
- and NADP-malate dehydrogenases, and alanine aminotransferase from epidermis and whole leaves was investigated. Short-term exposure to SO(2) at 0.2 or 0.5 ppm decreased the activity of the carboxylase and the dehydrogenases in the epidermis. In contrast, the activity of the same three enzymes increased in whole leaves with either short- or long-term exposure to SO(2). Alanine aminotransferase in epidermis or whole leaves was not much affected by short-term exposure, but the epidermal activity was decreased and whole leaf activity was increased with long-term exposure. SO(2) exposure which was initiated prior to illumination decreased the free thiol content of both epidermis and of whole leaf. Net photosynthesis was reversibly inhibited by long-term exposure to SO(2) at 0.5 ppm. No effect of 0.5 ppm SO(2) on stomatal conductance was detectable after 3 hours. Stomatal conductance appeared to decrease after longer exposure times (2 days) at 0.5 ppm.
...
PMID:Effects of SO(2) on Stomatal Metabolism in Pisum sativum L. 1666 45
Ribulose bisphosphate carboxylase/oxygenase (RuBPCase) from several plants had substantially greater activity in extracts from lightexposed leaves than dark leaves, even when the extracts were incubated in vitro with saturating HCO(3) (-) and Mg(2+) concentrations. This occurred in Glycine max, Lycopersicon esculentum, Nicotiana tabacum, Panicum bisulcatum, and P. hylaeicum (C(3)); P. maximum (C(4)
phosphoenolpyruvate carboxykinase
); P. milioides (C(3)/C(4)); and Bromelia pinguin and Ananas comosus (Crassulacean acid metabolism). Little or no difference between light and dark leaf extracts of RuBPCase was observed in Triticum aestivum (C(3)); P. miliaceum (C(4)
NAD
malic enzyme); Zea mays and Sorghum bicolor (C(4) NADP malic enzyme); Moricandia arvensis (C(3)/C(4)); and Hydrilla verticillata (submersed aquatic macrophyte). It is concluded that, in many plants, especially Crassulacean acid metabolism and C(3) species, a large fraction of ribulose-1,5-bisphosphate carboxylase/oxygenase in the dark is in an inactivatable state that cannot respond to CO(2) and Mg(2+) activation, but which can be converted to an activatable state upon exposure of the leaf to light.
...
PMID:Dark/Light modulation of ribulose bisphosphate carboxylase activity in plants from different photosynthetic categories. 1666 37
Light-induced swelling of guard cell protoplasts (GCP) from Vicia faba was accompanied by increases in content of K(+) and malate. DCMU inhibited the increase of K(+) and malate, and consequently swelling.Effect of light on the activity of selected enzymes that take part in malate formation was studied. When isolated GCP were illuminated, NADP-malate dehydrogenase (NADP-MDH) was activated, and the activity reached a maximum within 5 minutes. The enzyme activity underwent 5- to 6-fold increase in the light. Upon turning off the light, the enzyme was inactivated in 5 minutes
NAD
-MDH and
phosphoenolpyruvate carboxylase
(
PEPC
) were not influenced by light. The rapid light activation of NADP-MDH was inhibited by DCMU, suggesting that the enzyme was activated by reductants from the linear electron transport in chloroplasts. An enzyme localization study by differential centrifugation indicates that NADP-MDH is located in the chloroplasts,
NAD
-MDH in the cytosol and mitochondria, and
PEPC
in the cytosol. After light activation, the activity of NADP-MDH in guard cells was 10 times that in mesophyll cells on a chlorophyll basis. The physiological significance of light-dependent activation of NADP-MDH in guard cells is discussed in relation to stomatal movement.
...
PMID:Light Activation of NADP-Malate Dehydrogenase in Guard Cell Protoplasts from Vicia faba L. 1666 99
Two naturally occurring species of the genus Alternanthera, namely A. ficoides and A. tenella, were identified as C(3)-C(4) intermediates based on leaf anatomy, photosynthetic CO(2) compensation point (Gamma), O(2) response of small ghe, Cyrillic, light intensity response of small ghe, Cyrillic, and the activities of key enzymes of photosynthesis. A. ficoides and A. tenella exhibited a less distinct Kranz-like leaf anatomy with substantial accumulation of starch both in mesophyll and bundle sheath cells. Photosynthetic CO(2) compensation points of these two intermediate species at 29 degrees C were much lower than in C(3) plants and ranged from 18 to 22 microliters per liter. Although A. ficoides and A. tenella exhibited similar intermediacy in small ghe, Cyrillic, the apparent photorespiratory component of O(2) inhibition in A. ficoides is lower than in A. tenella. The small ghe, Cyrillic progressively decreases from 35 microliters per liter at lowest light intensity to 18 microliters per liter at highest light intensity in A. tenella. It was, however, constant in A. ficoides at 20 to 25 microliters per liter between light intensities measured. The rates of net photosynthesis at 21% O(2) and 29 degrees C by A. ficoides and A. tenella were 25 to 28 milligrams CO(2) per square decimeter per hour which are intermediate between values obtained for Tridax procumbens and A. pungens, C(3) and C(4) species, respectively. The activities of key enzymes of C(4) photosynthesis,
phosphoenolpyruvate carboxylase
, pyruvate Pi dikinase,
NAD
malic enzyme, NADP malic enzyme and
phosphoenolpyruvate carboxykinase
in the two intermediates, A. ficoides and A. tenella are very low or insignificant. Results indicated that the relatively low apparent photorespiratory component in these two species is presumably the basis for the C(3)-C(4) intermediate photosynthesis.
...
PMID:C(3)-C(4) Intermediate Species in Alternanthera (Amaranthaceae) : Leaf Anatomy, CO(2) Compensation Point, Net CO(2) Exchange and Activities of Photosynthetic Enzymes. 1666 34
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