Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:4.1.2.13 (aldolase)
3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Glycogen content and the activities of phosphorylase, phosphohexose isomerase, aldolase, glucose 6-phosphatase, succinate dehydrogenase, and alanine and aspartate amino-transferases have been biochemically determined in three gastrocnemii muscles of chick up to 9 weeks of postembryonic growth. Decline in glycogen, phosphorylase, phosphohexose isomerase and aldolase with a concomitant increase in succinate dehydrogenase reveals a switchover from glycolytic to oxidative metabolism in muscle. Activities of aminotransferases indicate the utilization of transamination products of alanine and aspartate in oxidative pathway. Transiently increased glucose 6-phosphatase seems to restrict glycogenolytic and glycolytic metabolism and thereby pave way for the acceleration of oxidative metabolism in developing muscle.
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PMID:Does glucose 6-phosphatase regulate metabolic transformation in developing skeletal muscle? 633 26

Mutant cells of mucoid Pseudomonas aeruginosa isolated from cystic fibrosis patients were examined for their ability to synthesize alginic acid in resting cell suspensions. Unlike the wild-type strain which synthesizes alginic acid from glycerol, fructose, mannitol, glucose, gluconate, glutamate, or succinate, mutants lacking specific enzymes of carbohydrate metabolism are uniquely impaired. A phosphoglucose isomerase mutant did not synthesize the polysaccharide from mannitol, nor did a glucose 6-phosphate dehydrogenase mutant synthesize the polysaccharide from mannitol or glucose. Mutants lacking the Entner-Doudoroff pathway dehydrase or aldolase failed to produce alginate from mannitol, glucose, or gluconate, as a 3-phosphoglycerate kinase or glyceraldehyde 3-phosphate dehydrogenase mutant failed to produce from glutamate or succinate. These results demonstrate the primary role of the Entner-Doudoroff pathway enzymes in the synthesis of alginate from glucose, mannitol, or gluconate and the role of glyceraldehyde 3-phosphate dehydrogenase reaction for the synthesis from gluconeogenic precursors such as glutamate. The virtual absence of any activity of phosphomannose isomerase in cell extracts of several independent mucoid bacteria and the impairment of alginate synthesis from mannitol in mutants lacking phosphoglucose isomerase or glucose 6-phosphate dehydrogenase rule out free mannose 6-phosphate as an intermediate in alginate biosynthesis.
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PMID:Alginic acid synthesis in Pseudomonas aeruginosa mutants defective in carbohydrate metabolism. 640 61

The significance of changes in lymph flow for the extracellular distribution and transport of cellular enzymes and for the level of enzyme activities in plasma was investigated. Specimens of thoracic duct lymph were obtained from an extracorporal lymph shunt in anaesthetized, conscious resting and treadmill exercising dogs (6 km X h-1 for 1 h) The activity of 10 enzymes and of protein content in lymph and plasma were studied, as well as lymph flow, lymphatic transport, and the lymph-plasma ratio of these compounds. Lactate, pH, and blood gases were monitored in venous blood. Lymph flow of 0.80 ml X min-1 in anaesthetized dogs more than doubled (to 1.86 ml X min-1) when the animals were conscious and resting. In anaesthetized dogs lymph enzyme activity was higher only for enzymes of predominately hepatic origin, such as choline esterase (CHE) and alanine aminoferase (ALAT), and was lower for aspartate aminotransferase (ASAT) and aldolase (ALD). In conscious dogs, due to activation of the skeletal muscle "tissue pump", lymphatic transport of enzymes with rather high activity in skeletal muscle, and of protein, is significantly enhanced. Enzyme activities in plasma, however, did not differ between the groups. Lymph-plasma activity ratios higher than one were found for lactate dehydrogenase (LDH), malate dehydrogenase (MDH), ASAT, creatine kinase (CK), ALD, and phosphohexose isomerase (PHI). Exercise stimulated lymph flow up to 4.9 ml X min-1, and increased the lymphatic activities of those enzymes with a lymph-plasma ratio higher than unity, these enzymes increasing in the plasma due to the highly increased lymphatic transport.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzyme activities in thoracic duct lymph and plasma of anaesthetized, conscious resting and exercising dogs. 642 59

Evidence is presented for the occurrence of glycosomes (organelles resembling peroxisomes) in four major species of Leishmania (viz. L. major, L.m. mexicana, L. b. braziliensis and L. donovani), based on latency as well as differential and isopycnic centrifugation studies. The enzymes involved in glycolysis; (hexokinase, phosphoglucose isomerase, phosphofructokinase, fructose-1,6-bisphosphate aldolase, triosephosphate isomerase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase); glycerol metabolism (sn-glycerol-3-phosphate dehydrogenase and glycerol kinase); carbon dioxide fixation (phosphoenolpyruvate carboxykinase and possibly malate dehydrogenase); together with an enzyme involved in the beta-oxidation of fatty acids (3-beta-hydroxybutyryl coenzyme A dehydrogenase); a key enzyme in the synthesis of ether lipids (dihydroxyacetone phosphate acyltransferase) as well as the ADP utilising enzyme adenylate kinase, were all found associated, at least in part, with a subcellular organelle which had a buoyant density in sucrose gradients of 1.21 to 1.24 g cm-3. Little variance in enzyme composition was found between the different species of Leishmania or in comparison with other members of the Trypanosomatidae, supporting the unifying principle that glycosomes are a unique characteristic of this family. The occurrence of important catabolic, anabolic and anaplerotic pathways in the glycosomes of Leishmania renders them prime targets for chemotherapy.
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PMID:The occurrence of glycosomes (microbodies) in the promastigote stage of four major Leishmania species. 644 18

Highly purified glycosomes were isolated from Trypanosoma brucei bloodstream forms and cultured procyclic trypomastigotes. A comparison of the specific activities of glycosomal enzymes revealed that glycosomes from insect stages had decreased levels of hexokinase, phosphoglucose isomerase, phospho-fructokinase, fructose-bisphosphate aldolase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase, but contained increased levels of adenylate kinase, malate dehydrogenase and phosphoenolpyruvate carboxykinase. Glycosomes from bloodstream forms were almost totally devoid of the latter two activities. Comparison of the two types of glycosomes by sodium dodecylsulphate-polyacrylamide gel electrophoresis revealed that bloodstream form glycosomes contained 3 prominent polypeptides (64, 46 and 40 kDa) which were hardly detectable in insect stage glycosomes, whereas the latter contained 3 insect stage specific bands with molecular weight of 34 000, 61 000 and 77 000 and 4 additional bands with molecular weights between 94 000 and 110 000. Both types of glycosome contained the phospholipids phosphatidylcholine and phosphatidylethanolamine. Insect stage glycosomes contained in addition also phosphatidylinositol and some phosphatidylserine.
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PMID:A comparison of the glycosomes (microbodies) isolated from Trypanosoma brucei bloodstream form and cultured procyclic trypomastigotes. 674 87

The activities of 13 liver and 6 brain enzymes were studied in 7-12 week old CD2F1 male mice that had been fed ad libitum and standardized either to 12 hours of light (0600-1800) alternating with 12 hours of darkness (1800-0600) (LD12:12); or to a reversed light-dark cycle (darkness 0600-1800; light 1800-0600) (DL12:12). Three separate studies were performed on two different days; in each experiment, subgroups of 14 animals were sacrificed at 3-hour intervals. Livers were assayed for: isocitrate dehydrogenase, glutamate dehydrogenase, lactate dehydrogenase, alcohol dehydrogenase, glutathione reductase, glyoxylate reductase, L-alanine aminotransferase, glutamate oxalacetate transaminase, pyruvate decarboxylase, fructose-1-phosphate aldolase, fructose diphosphate aldolase, fructose 1,6-diphosphatase, and fatty acid synthetase. Brains were assayed for phosphoglucose isomerase, adenosine triphosphatase, creatine phosphokinase, pyruvate kinase, adenylate kinase, and malate dehydrogenase. All 19 enzymes demonstrated a prominent circadian rhythm in at least one experiment. Moreover, each rhythmic variable showed a statistically significant fit to a 24-hour cosine (sine) curve by the method of least squares. In general, peak activities of the liver enzymes analyzed were associated with the beginning of the dark cycle and initiation of the animal's activity, while the group of brain enzymes had peak activities which occurred at the beginning of the animals' rest span and were near the beginning of the light cycle. The phasing of each of the rhythms could be reversed within a two-week span after reversing the environmental light-dark cycle 180 degrees.
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PMID:Circadian organization of thirteen liver and six brain enzymes of the mouse. 731 49

Several glycolytic enzymes exist in muscle as free and structure-bound forms. A fraction of hexokinase (HK) is associated with the outer mitochondrial membrane. Phosphofructokinase (PFK) and aldolase (ALD) bind to F-actin, and AMP deaminase (AMPase) interacts with myosin. Using low-frequency stimulation (10 Hz, 24 h/d), we studied in rat fast-twitch muscle effects of contractile activity on soluble and structure-bound forms of these enzymes. Phosphoglucose isomerase (PGI), a soluble enzyme, was also examined. Fractional extraction was applied to study the intracellular distribution of soluble and bound enzyme activities 5 min, 1 h, 3 h, 1 d, and 7 d after the onset of stimulation. Confirming previous findings, total HK activity increased 7-fold in 7-d-stimulated muscles, whereas PFK, ALD, and PGI were reduced, ranging between 55% and 80% of their normal activities. AMPase activity was unaltered. At the time points studied, no changes were found in the extraction behavior of PGI and AMPase. The fraction of bound ALD increased slightly (12%). However, the distribution of HK and PFK was markedly altered. Bound PFK increased from 50% in the control to 85% in 7-d-stimulated muscles. Bound HK rose from 52% to 83% during the same time period. The increase in PFK binding was steep and occurred mainly within the first minutes and hours. The increase in HK binding occurred with some delay, but was significant in muscles stimulated for more than 1 h. In view of the altered kinetic properties of F-actin-bound PFK (alleviated allosteric inhibition by ATP) and bound HK (elevated catalytic activity), these changes are interpreted as early responses to match the metabolic demands during maximal contractile activity imposed on a muscle not programmed for sustained activity: Enhanced binding of PFK serves to accelerate glycolytic flux immediately after the onset of stimulation, whereas mitochondrial binding of HK facilitates the phosphorylation of exogenous glucose when glycogen stores have been depleted.
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PMID:Effects of low-frequency stimulation on soluble and structure-bound activities of hexokinase and phosphofructokinase in rat fast-twitch muscle. 766 4

The main pathway for the fermentation of maltose or cellobiose by the hyperthermophile Pyrococcus furiosus was investigated by in vivo NMR and by enzyme measurements. Addition of [1-13C]glucose to cell suspensions resulted in the formation of C2-labeled acetate and C3-labeled alanine. No label was recovered in CO2 or HCO3-. In the presence of [3-13C]glucose, the label ended up in the C1 atom of alanine and in HCO3- and CO2. These labeling patterns indicate that glucose is converted along an Embden-Meyerhof pathway, and they disagree with the previously proposed nonphosphorylated Entner-Doudoroff pathway (pyroglycolysis). The NMR data were supported by enzyme measurements. Hexokinase (8.7 units/mg), phosphoglucose isomerase (6.8 units/mg), phosphofructokinase (0.81 unit/mg), and aldolase (0.26 unit/mg) were present in cell-free extracts (specific activities at 90 degrees C). Remarkably, the two kinases required ADP as the phosphoryl group donor instead of ATP. No activity was found with pyrophosphate. These are the first descriptions of ADP-dependent (AMP-forming) kinases to date. Since P. furiosus is a phylogenetically ancient organism, these enzymes may represent an ancestral kind of metabolism.
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PMID:Evidence for the operation of a novel Embden-Meyerhof pathway that involves ADP-dependent kinases during sugar fermentation by Pyrococcus furiosus. 802 Dec 61

Enzymology has acquired a prominent place in human pathology, and serum enzyme investigations have become a prerequisite for various diseases, including cancer. Serum phosphohexose isomerase (PHI), aldolase (ALD) and alkaline phosphatase (ALP) levels were evaluated in 90 untreated patients with cervical carcinoma and 84 healthy age-matched females (controls). The concentrations of the three enzymes were significantly raised (p < 0.001) in patients compared to the controls. Receiver operating characteristic curve analysis revealed higher sensitivities of PHI and ALP, as compared to ALD at different specificity levels between 60 and 95%. Combined use of PHI and ALP revealed increased sensitivity and specificity. Combined use of PHI, ALD and ALP revealed a greater number of responders with enzyme values within the normal range than nonresponders. The results suggest that combined evaluation of the enzymes might be helpful to establish a useful aid to strengthen the armamentarium currently employed in the diagnosis and treatment monitoring of patients with cervical carcinoma.
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PMID:Combined use of serum enzyme levels as tumor markers in cervical carcinoma patients. 814 29

Methanococcus maripaludis, a facultatively autotrophic archaebacterium that grows with H2 or formate as the electron donor, does not assimilate sugars and other complex organic substrates. However, glycogen is biosynthesized intracellularly and commonly reaches values of 0.34% of the cellular dry weight in the early stationary phase. To determine the pathway of glycogen catabolism, specific enzymes of sugar metabolism were assayed in cell extracts. The following enzymes were found (specific activity in milliunits per milligram of protein): glycogen phosphorylase, 4.4; phosphoglucomutase, 10; glucose-6-phosphate isomerase, 9; 6-phosphofructokinase, 5.6, fructose-1,6-bisphosphatase, 10; fructose-1,6-bisphosphate aldolase, 4.2; triosephosphate isomerase, 44; glyceraldehyde-3-phosphate dehydrogenase, 26; phosphoglycerate kinase, 20; phosphoglycerate mutase, 78; enolase, 107; and pyruvate kinase, 4.0. Glyceraldehyde-3-phosphate dehydrogenase was NADP+ dependent, and the pyruvate kinase required MnCl2. The 6-phosphofructokinase had an unusually low pH optimum of 6.0. Four nonoxidative pentose-biosynthetic enzymes were found (specific activity in milliunits per milligram of protein): transketolase, 12; transaldolase, 24; ribulose-5-phosphate-3-epimerase, 55; and ribulose-5-phosphate isomerase, 100. However, the key enzymes of the oxidative pentose phosphate pathway, the reductive pentose phosphate pathway, and the classical and modified Entner-Duodoroff pathways were not detected. Thus, glycogen appears to be catabolized by the Embden-Meyerhoff-Parnas pathway. This result is in striking contrast to the nonmethanogenic archaebacteria that have been examined, among which the Entner-Doudoroff pathway is common. A dithiothreitol-specific NADP(+)-reducing activity was also found (8.5 mU/mg of protein). Other thiol compounds, such as cysteine hydrochloride, reduced glutathione, and 2-mercaptoethanesulfonic acid, did not replace dithiothreitol for this activity. The physiological significance of this activity is not known.
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PMID:Pathway of glycogen metabolism in Methanococcus maripaludis. 828 25


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