Gene/Protein Disease Symptom Drug Enzyme Compound
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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)

It has previously been suggested that the synthesis of phosphoenolpyruvate carboxykinase (EC 4.1.1.32) in Aspergillus nidulans is regulated by a repression-derepression mechanism involving a glycolytic intermediate, and not by induction. Results obtained using compounds that enter the tricarboxylic acid cycle via 2-oxoglutarate, and that can supply both a carbon and a nitrogen source for A. nidulans, suggest it is more likely that the synthesis of phosphoenolpyruvate carboxykinase is inducible, and only weakly regulated by carbon catabolite repression. a similar study of the regulation of the NADP-linked malic enzyme (EC 1.1.1.40) indicates that it too may be inducible.
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PMID:The regulation of phosphoenolpyruvate carboxykinase and the NADP-linked malic enzyme in Aspergillus nidulans. 703 61

1. The physiological response of rainbow trout (Salmo gairdneri) reared on different levels of available carbohydrate in practical trout diets having the same levels of energy and nitrogen for 16-24 weeks was determined. 2. Weight gain was significantly reduced in trout reared on the highest level of available carbohydrate, 210 g cerelose (alpha-glucose) kg, and there was a significant linear regression (R2 0.88 of dietary carbohydrate on weight gain. 3. Liver: body-weight values and liver glycogen levels increased in relation to increased dietary carbohydrate. 4. Liver glucose-6-phosphate dehydrogenase (EC 1.1.1.49) activity increased and liver phosphoenolpyruvate carboxykinase (EC 4.1.1.32) activity decreased per kg body-weight of fish with increasing dietary carbohydrate. However, no significant effect was noted on the activity of these liver enzymes above a dietary cerelose level of 140 g/kg. 5. Liver fructose diphosphatase (EC 3.1.3.11) activity increased with increasing dietary carbohydrate has been interpreted as meaning a recycling of triosephosphate to glucose-6-phosphate. 6. Dietary carbohydrate level had no significant effect on the liver pyruvate kinase (EC 2.7.1.40) activity, the rate of glucose utilization or the percentage conversion of [14C]alanine to glucose in the plasma of trout. 7. The results indicate that rainbow trout have a limited ability to adapt to increased dietary carbohydrate and a level in excess of 140 g/kg of the diet is not efficiently utilized.
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PMID:Response of rainbow trout (Salmo gairdneri) to increased levels of available carbohydrate in practical trout diets. 708 28

Panicum miliaceum has at least three isozymes of aspartate aminotransferase (AspAT); the cytosolic and mitochondrial isozymes (cAspAT and mAspAT) are major components and the third is a minor isozyme. Fractionation of leaf subcellular components showed that the minor isozyme was localized in plastids (pAspAT). We purified the three isozymes from green leaves of P. miliaceum. Both cAspAT and pAspAT consisted of triple subforms having the same molecular size but different isoelectric points. No substantial difference in enzymatic properties was observed among these isozymes besides the pH profiles. We isolated a full-length cDNA clone for pAspAT. This clone contains an open reading frame that encodes 457 amino acids. The amino-terminal region of the pAspAT precursor shares common features of plastid transit peptides. The amino acid sequence of P. miliaceum pAspAT shows higher similarity with other plant pAspATs than P. miliaceum cAspAT and mAspAT. The mRNA levels of the three isozymes were high in leaves compared with roots and mesocotyls. The three isozymes showed different expression patterns against environmental stimuli such as light and nitrate. The activities and protein levels of cAspAT and mAspAT increased during greening in accordance with those of phosphoenolpyruvate carboxylase and NAD-malic enzyme involved in the C4 pathway, primarily as a consequence of the increase in the levels of their mRNAs. By contrast, pAspAT was constitutively expressed during greening. The activity and protein levels of cAspAT and mAspAT selectively increased during recovery from an nitrogen deficit, primarily as a consequence of increase in the levels of their mRNAs while those of pAspAT remained unchanged.
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PMID:Aspartate aminotransferase isozymes in Panicum miliaceum L., an NAD-malic enzyme-type C4 plant: comparison of enzymatic properties primary structures, and expression patterns. 773 57

The goal of this study was to localize phosphoenolpyruvate carboxykinase (PEPCK), glycogen synthase (GS), and glycogen phosphorylase (GP) in the liver lobule by immunocytochemical techniques and to describe the effects of feeding and fasting on the distribution and quantity of these enzymes. Livers from ad lib fed and overnight fasted normal adult male rats were frozen in liquid nitrogen after transcardial perfusion with 30% sucrose. Serial cryostat sections of tissue were collected on slides, fixed by immersion in 4% paraformaldehyde, and incubated with antibodies against PEPCK, GS, and GP. Antibodies to these enzymes were visualized with a gold-conjugated secondary antibody and a silver enhancement technique. Fed animals demonstrated a periportal to pericentral gradient of PEPCK. Fasting increased the periportal content of PEPCK, induced the midlobular and centrilobular cells to express the enzyme, and steepened the periportal to pericentral gradient. The increase of PEPCK was confirmed by Western blot analysis. GS and GP were distributed throughout the lobule in the fed animal but often showed a centrilobular pattern, and fasting did not alter the lobular distribution of either enzyme. Western blot analysis revealed no changes in the amount of these enzymes in the fed or fasted state. The cellular distribution of the three enzymes is similar to that of hepatic glycogen, in that the immunoreactive material has a clumped appearance in the periportal hepatocytes and is more dispersed in the pericentral cells. On fasting the periportal hepatocytes lose the dense compact localization of the enzymes and the protein becomes more homogeneously distributed throughout the cytosol. Further studies are needed to elucidate the functional significance of the regional heterogeneity of the glycogen-metabolizing enzymes and the molecular mechanisms regulating their gene expression.
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PMID:Hepatic lobular patterns of phosphoenolpyruvate carboxykinase, glycogen synthase, and glycogen phosphorylase in fasted and fed rats. 824 33

Although housekeeping functions have been shown for the phosphoenolpyruvate carboxylase (EC 4.1.1.31, PEPC) in plants and in prokaryotes, PEPC is mainly known for its specific role in the primary photosynthetic CO2 fixation in C4 and CAM plants. We have shown that in Sorghum, a monocotyledonous C4 plant, the enzyme is encoded in the nucleus by a small multigene family. Here we report the entire nucleotide sequence (7.5 kb) of the third member (CP21) that completes the structure of the Sorghum PEPC gene family. Nucleotide composition, CpG islands and GC content of the three Sorghum PEPC genes are analysed with respect to their possible implications in the regulation of expression. A study of structure/function and phylogenetic relationships based on the compilation of all PEPC sequences known so far is presented. Data demonstrated that: (1) the different forms of plant PEPC have very similar primary structures, functional and regulatory properties, (2) neither apparent amino acid sequences nor phylogenetic relationships are specific for the C4 and CAM PEPCs and (3) expression of the different genes coding for the Sorghum PEPC isoenzymes is differently regulated (i.e. by light, nitrogen source) in a spatial and temporal manner. These results suggest that the main distinguishing feature between plant PEPCs is to be found at the level of genes expression rather than in their primary structure.
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PMID:Sorghum phosphoenolpyruvate carboxylase gene family: structure, function and molecular evolution. 844 42

The regulation of the supply of oxaloacetate (OAA) for mitochondrial metabolism via phosphoenolpyruvate carboxylase (PEPC) by covalent modification is studied in barley (Hordeum vulgare L.) leaf protoplasts in light or darkness as well as under photorespiratory or non-photorespiratory conditions. Extracts for studies on in vivo PEPC phosphorylation were prepared from barley leaf protoplasts by rapid filtration, fractionating the cell within less than 1 s. Measurements of in vitro PEPC activity were performed on samples quickly frozen in liquid nitrogen to break the cell and stop metabolism and thus preserve the in vivo activation state. The relative PEPC phosphorylation state increased upon illumination and decreased upon redarkening under photorespiratory and non-photorespiratory conditions. PEPC activity measured in the presence of malate (3 mM) under photorespiratory conditions showed the same response indicating that a light-induced increase in PEPC activity and decrease in malate sensitivity is caused by an increased phosphorylation level of the PEPC protein. PEPC activity was pH dependent. At the physiological cytosolic pH, activity was suboptimal, but most sensitive towards malate inhibition and glucose 6-phosphate stimulation. The presence of malate increased the sensitivity of PEPC activity towards pH changes. The response of PEPC activity to changing pH was not affected by changes in the activation state of the enzyme. The Km (phosphoenolpyruvate, PEP) is about 1 mM. Upon illumination the Km (PEP) decrease significantly. Vmax was unaffected by the light treatment. The presence of physiological concentrations of glucose 6-phosphate decreased Km (PEP) 5- to 10-fold and increased Vmax by about 35%. The effect of glucose 6-phosphate was strongest (up to 7-fold) at subsaturating PEP concentrations stimulating PEPC activity to nearly maximal rates. The results show that an increase in PEPC phosphorylation state causes an increase in PEPC activity as well as in substrate affinity leading to an increased production of OAA in the light.
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PMID:Regulation of the supply of cytosolic oxaloacetate for mitochondrial metabolism via phosphoenolpyruvate carboxylase in barley leaf protoplasts. I. The effect of covalent modification on PEPC activity, pH response, and kinetic properties. 862 18

The regulation of the supply of oxaloacetate (OAA) for mitochondrial metabolism via phosphoenolpyruvate carboxylase (PEPC) by metabolites is studied in barley (Hordeum vulgare L.) leaf protoplasts in light or darkness as well as under photorespiratory or non-photorespiratory conditions. Measurements on PEPC activity were performed on samples quickly frozen in liquid nitrogen to break the cell and stop metabolism and thus preserve the in vivo activation state. Glycine, serine, pyruvate, acetyl-CoA, glycolate, fructose 1,6-bisphosphate, fructose 2,6-bisphosphate and ADP had no significant effect on PEPC activity. Malate, aspartate and glutamate were strong inhibitors of PEPC activity decreasing the activity more in light versus darkness. However, at the physiological cytosolic concentration of these metabolites under the respective conditions, inhibition of PEPC activity was about the same with the exception of aspartate which inhibits more under non-photorespiratory than under photorespiratory conditions. 2-Oxoglutarate and glyoxylate decreased PEPC activity by 20 to 40% in the range of its physiological cytosolic concentration. Inhibition by physiological cytosolic concentrations of glutamine was limited. Glucose 6-phosphate, fructose 6-phosphate, 3-phosphoglycerate, dihydroxyacetonphosphate and P(i) stimulated PEPC activity significantly in their physiological cytosolic concentration range. Physiological cytosolic concentrations of glucose 6-phosphate and fructose 6-phosphate activated PEPC activity to about the same extent under all conditions applied, while 3-phosphoglycerate and dihydroxyacetonphosphate stimulating stronger under non-photorespiratory versus photorespiratory conditions. Moreover, dihydroxyacetonphosphate stimulated PEPC activity more in light versus darkness under non-photorespiratory conditions. P(i) activation of PEPC activity decreases in light versus darkness under non-photorespiratory conditions. Stimulation of PEPC activity by citrate in its physiological concentration range is limited. Glucose 1-phosphate and AMP activated PEPC activity only at concentrations higher than their physiological levels in the cytosol. Determinations of PEPC activity in the presence of different malate/glucose 6-phosphate ratios revealed that glucose 6-phosphate totally relieved the inhibitory effect of malate. The regulatory properties of PEPC activity will be discussed in relation to its functions in C3 plants.
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PMID:Regulation of the supply of oxaloacetate for mitochondrial metabolism via phosphoenolpyruvate carboxylase in barley leaf protoplasts. II. Effects of metabolites on PEPC activity at different activation states of the protein. 862 19

Sea raven (Hemitripterus americanus) given intraperitoneal implants of coconut oil containing cortisol (50 mg kg-1) and sampled 5 days later had plasma cortisol, glucose and urea concentrations higher than in a sham-implanted group. No differences in plasma ammonia, free amino acid or fatty acid concentrations were apparent between the cortisol- and sham-treated groups. There was no change in hepatic glycogen content, whereas glutamine synthetase, allantoicase, arginase, aspartate aminotransferase, tyrosine aminotransferase, alanine aminotransferase, glutamate dehydrogenase, phosphoenolpyruvate carboxykinase and 3-hydroxyacyl-coenzyme A dehydrogenase activities were higher in the cortisol-treated fish liver compared with the sham-implanted fish. On the basis of these general increases in enzyme activities, our results suggest that cortisol stimulates nitrogen metabolism in the sea raven. Amino acid catabolism may be a major source of substrate for gluconeogenesis and/or oxidation, while fatty acid mobilization may provide the fuel for endogenous use by the liver in cortisol-treated sea raven. These results further support the hypothesis that cortisol plays a role in the regulation of glucose production in stressed fish.
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PMID:Metabolic effects of cortisol treatment in a marine teleost, the sea raven 931 10

Unlike other lactic acid bacteria, Lactococcus lactis subsp. lactis NCDO 2118 was able to grow in a medium lacking glutamate and the amino acids of the glutamate family. Growth in such a medium proceeded after a lag phase of about 2 days and with a reduced growth rate (0.11 h-1) compared to that in the reference medium containing glutamate (0.16 h-1). The enzymatic studies showed that a phosphoenolpyruvate carboxylase activity was present, while the malic enzyme and the enzymes of the glyoxylic shunt were not detected. As in most anaerobic bacteria, no alpha-ketoglutarate dehydrogenase activity could be detected, and the citric acid cycle was restricted to a reductive pathway leading to succinate formation and an oxidative branch enabling the synthesis of alpha-ketoglutarate. The metabolic bottleneck responsible for the limited growth rate was located in this latter pathway. As regards the synthesis of glutamate from alpha-ketoglutarate, no glutamate dehydrogenase was detected. While the glutamate synthase-glutamine synthetase system was detected at a low level, high transaminase activity was measured. The conversion of alpha-ketoglutarate to glutamate by the transaminase, the reverse of the normal physiological direction, operated with different amino acids as nitrogen donor. All of the enzymes assayed were shown to be constitutive.
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PMID:Glutamate Biosynthesis in Lactococcus lactis subsp. lactis NCDO 2118 964 19

To analyze the role of phosphoenolpyruvate carboxylase (PEPCase, EC 4.1.1.31) during seed development, two cDNA clones encoding two isoforms of PEPCase were isolated from a seed-specific library of Vicia faba. The two sequences (VfPEPCase1 and VfPEPCase2) have a sequence identity of 82 and 89% on the nucleotide and amino acid levels. The VfPEPCase1 mRNA was found to be predominantly expressed in roots and developing cotyledons whereas the VfPEPCase2 mRNA was more abundant in green and maternal tissues. In the cotyledons, PEPCase mRNAs accumulated from early to mid cotyledon stage and decreased thereafter. The PEPCase activity increased continuously during cotyledon development. The enzyme was strongly activated by glucose-6-phosphate, but not by glucose, fructose or sucrose. Asparagine was weakly activating whereas malate, aspartate and glutamate were inhibitory. The inhibitors became less effective with increasing pH. Aspartate was a much stronger inhibitor of cotyledonary PEPCase than glutamate at both pH 7.0 and 7.5. The sensitivity of PEPCase to malate inhibition decreased from early to mid cotyledon stage at a time when storage proteins are synthesized. This indicates activation on the protein level, possibly by protein phosphorylation. Nitrogen starvation in the presence of hexoses but not sucrose decreased mRNA levels of VfPEPCase1 and enzyme activity, indicating control on the mRNA level by both carbon and nitrogen. It is concluded that in developing cotyledons PEPCase is probably important for the synthesis of organic acids to provide carbon skeletons for amino acid synthesis.
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PMID:Phosphoenolpyruvate carboxylase in developing seeds of Vicia faba L.: gene expression and metabolic regulation. 1021 2


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