Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.4.1.1 (pyruvate carboxylase)
 1,516 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Optimal concentrations of the essential components for analyzing the activity of each enzyme associated with glycolysis and gluconeogenesis in rabbit periodontal ligament were examined, and enzyme assay systems for 15 enzymes including 22 reactions were established using triethanolamine buffer. Specific activities of all the enzymes, except for the gluconeogenic reaction of phosphoglycerate kinase, were systematically evaluated using the optimum buffer for each enzyme, since the activity of each enzyme varied depending on the buffer used. For glycolysis, the activity levels of hexokinase and 6-phosphofructokinase were very low, and consequently these enzyme reactions were inferred to be the rate-limiting steps. For gluconeogenesis, fructose 1,6-bisphosphatase and aldolase activities were extremely low, and the activities of glucose 6-phosphatase, phosphoenolpyruvate carboxykinase and pyruvate carboxylase were undetectable. These results suggest that the periodontal ligament may have no gluconeogenesis capability. With a rise in pH, the activities of the key enzymes of glycolysis gradually increased, and a specific "crossover" point was found between the activities of glyceraldehyde-phosphate dehydrogenase and phosphoglyceromutase. In addition, the activity of fructose 1,6-bisphosphatase, one of the key enzymes of gluconeogenesis, was markedly increased with a rise in pH, although pH changes had no effect on aldolase activity. Consequently, alkaline pH appeared to result in overall stimulation of glycolysis.
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PMID:Enzymatic regulation of glycolysis and gluconeogenesis in rabbit periodontal ligament under various physiological pH conditions. 165 53

(1) Liver cells from starved rats were incubated with 10 mM L-lactate, 1 mM pyruvate and 0.3 microM glucagon in the presence and absence of the mild respiratory inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) at 0.5 mM. (2) The whole cell concentrations of phosphoenolpyruvate, 2-phosphoglycerate and 3-phosphoglycerate increased about 2-fold, whilst the triose and hexose phosphate concentrations all decreased significantly. Similar results were obtained with 0.15 microM oligomycin and 10 microM atractyloside. (3) These data can be explained by a substantial decrease in the cytosolic free concentration ratio of ATP/ADP acting on the equilibrium of glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase. (4) The increase in cytosolic phosphoenolpyruvate concentration can account for the observed increase in pyruvate kinase flux that occurs under these conditions (Pryor et al. (1987) Biochem. J. 247, 449-457). (5) An inhibition of pyruvate carboxylase was also implied by a decrease in calculated tissue oxaloacetate concentrations, confirming a role for both enzymes in the inhibition of gluconeogenesis. (6) Whole cell concentrations of effectors of pyruvate carboxylase activity were measured; only the ATP/ADP ratio decreased significantly. (7) Subcellular fractionation studies showed a good correlation between the measured mitochondrial ATP/ADP ratio and rates of gluconeogenesis both in the presence and absence of oleate. (8) A similar correlation could be observed between rates of pyruvate carboxylation and the measured matrix ATP/ADP ratio in isolated liver mitochondria from starved rats. (9) Data are also presented suggesting an additional effect of DCMU on the rate pyruvate carboxylation in situ under some circumstances, mediated by decreases in mitochondrial acetyl-CoA and cytosolic pyruvate concentrations. (10) It is noted that the effects of phenylethylbiguanide (phenformin) on the rate of gluconeogenesis and metabolite profiles in the perfused liver (Cooke et al. (1973) J. Biol. Chem. 248, 5272-5277) are similar to those caused by DCMU, supporting a mitochondrial locus of action for this hypoglycaemic agent.
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PMID:The mechanisms by which mild respiratory chain inhibitors inhibit hepatic gluconeogenesis. 845 80

Enzymatic activities of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) (EC 4.1.1.39), phospho(enol)pyruvate carboxylase (EC 4.1.1.31), NAD malate dehydrogenase (EC 1.1.1.37), and NADP glyceraldehydephosphate dehydrogenase complex including phosphoglycerate kinase (EC 2.7.2.3) and glyceraldehydephosphate dehydrogenase (EC 1.2.1.13) were comparatively assayed in wheat seedlings of the cultivar Lyutestsens 758 grown under normal conditions, water deficiency conditions, and subsequent rehydration. Water stress was found to decrease the activity of all enzymes tested, the effect being most pronounced in case of Rubisco. The content of Rubisco in wheat plants exposed to water deficiency was reduced less significantly than the activity of the enzyme. Preliminary treatment of plant seeds with kartolin-4 (o-isopropyl-N-2-hydroxyethyl carbamate), a preparation with cytokinin activity, reduced the dehydration-induced inhibition of enzymatic activity. Upon a subsequent rehydration, kartolin-4 facilitated rapid recovery of the photosynthetic activity, the process being based on the kartolin-induced stimulation of reparation reactions. Under conditions of water stress, a partial decrease in the activity of carbon metabolism enzymes in vitro was accompanied by complete inhibition of photosynthesis in vivo, perhaps, as a result of an abrupt increase in the stomatal resistance.
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PMID:[Activity of carbon metabolism enzymes in wheat plants treated with kartolin-4 and exposed to water stress]. 1177 26

The effects of synthetic preparations exhibiting cytokinin-like activity (6-benzylaminopurine, Thidiazuron, and kartolin-2) on the specific leaf area (SLA) were studied in plants of the family Gramineae (wheat, Triticum aestivum L.; meadow fescue, Festuca pratensis Huds.; and reed fescue, F. arindinacea Schreb.). At the early stages of ontogeny (until the leaf area reached 50-60% of the maximum value), treatment of plants of the three species with cytokinin-like preparations caused an increase in SLA. The SLA value in these plants was correlated with the rate of photosynthetic assimilation of carbon dioxide and activities of carbon metabolism enzymes: ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39), NAD-malate dehydrogenase (EC 1.1.1.37), and NADP-glyceraldehydrophosphate dehydrogenase complex, which includes phosphoglycerate kinase (EC 2.7.2.3) and glyceraldehydrophosphate dehydrogenase (EC 1.2.1.13). However, there was no correlation of SLA with the activity of phospho(enol)pyruvate carboxylase (EC 4.1.1.31), an anaplerotic carboxylation enzyme of grasses. SLA is suggested to reflect the state and activity of the photosynthetic apparatus and can be recommended as a characteristic of photosynthesis variability (e.g., caused by cytokinin-like preparations).
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PMID:[Effect of preparations exhibiting cytokinin-like activity on the specific density of leaf in grasses]. 1244 1

Campylobacter contaminated poultry meat is a major source of human foodborne illness. Campylobacter coli strain OR12 is a robust colonizer of chickens that was previously shown to outcompete and displace other Campylobacter strains from the chicken's gastrointestinal tract. This strain is capable of aerobic growth on blood agar. Serial aerobic passage increased this aerotolerance as assessed by quantitative assays for growth and survival on solid media. Aerotolerance was also associated with increased peroxide stress resistance. Aerobic passage did not alter cellular morphology or motility or hinder the microaerobic growth rate. Colonization of broiler chickens by aerotolerant C. coli OR12 was significantly lower than the wild-type strain at 3 days after challenge but not by 7 days, suggesting adaptation had occurred. Bacteria recovered from chickens had retained their aerotolerance, indicating this trait is stable. Whole genome sequencing enabled comparison with the wild-type sequence. Twenty-three point mutations were present, none of which were in genes known to affect oxidative stress resistance. Insertions or deletions caused frame shifts in several genes including, phosphoglycerate kinase and the b subunit of pyruvate carboxylase that suggest modification of central and carbohydrate metabolism in response to aerobic growth. Other genes affected include those encoding putative carbonic anhydrase, motility accessory factor, filamentous haemagglutinin, and aminoacyl dipeptidase proteins. Aerotolerance has the potential to affect environmental success and survival. Increased environmental survival outside of the host intestinal tract may allow opportunities for transmission between hosts. Resistance to oxidative stress may equate to increased virulence by virtue of reduced susceptibility to oxidative free radicals produced by host immune responses. Finally, resistance to ambient atmospheric oxygen may allow increased survival on chicken skin, and therefore constitutes an increased risk to public health.
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PMID:Characterisation of Aerotolerant Forms of a Robust Chicken Colonizing Campylobacter coli. 2839 58