Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Concentrations of key metabolites were determined in carp white muscle before exercise and after maximal activity. It was found that the concentration of ATP decreases by about 65%, ADP decreases slightly, and AMP remains unchanged. Consequently, the level of the free adenylate pool decreases. Simultaneously there is an increase in the concentration of IMP and NH4+. The increase in IMP level and the decrease in adenylate pool are essentially in 1:1 stoichiometry, a result showing that the adenylate pool is decreased by the reaction catalyzed by 5'-AMP deaminase (EC 3.5.4.6.). During exercise there is an increase in levels of glucose-6-phosphate, fructose 6-phosphate, and fructose 1,6-diphosphate that, along with the decrease in ATP levels, can account for the increase in glycolytic flux by activation of phosphofructokinase and pyruvate kinase.
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PMID:Control of energy metabolism in fish white muscle. 13 93

Contemporary data on three enzymes of vertebrate cross-striated muscle thick filaments, such as creatine kinase, AMP-deaminase and phosphofructokinase, are reviewed. The physico-chemical, enzymatic and regulatory properties and localization of these enzymes in different zones of the thick filament are considered. The functional relevance of localization of creatine kinase, AMP-deaminase and phosphofructokinase on thick filaments is discussed in terms of the possible role of the enzyme adsorption on subcellular structures in regulation of metabolic processes.
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PMID:[Enzymes in thick filaments of vertebrate cross-striated muscles]. 129 52

This communication presents the results obtained in tubular aggregates of 24 enzyme histochemical techniques for demonstrating activity of oxidoreductases, transferases, hydrolases and isomerases. The activity characteristics of the tubular aggregates in m. gluteus medius of 18 patients with diseases of the neuromuscular system were almost identical. A high activity of the mitochondrial enzymes, NADPH: tetrazolium oxidoreductase, NADH:tetrazolium oxidoreductase and cytochrome c oxidase, could be shown in the pathological structures, whereas the activity of the mitochondrial enzymes, glycerol-3-phosphate:menadione oxidoreductase, succinate:PMS oxidoreductase, malate:NAD+ oxidoreductase and isocitrate:NAD+ oxidoreductase, and the partial mitochondrial enzymes, malate:NADP+ oxidoreductase and isocitrate:NADP+ oxidoreductase, was very slight or even absent. There was a moderate to strong activity of the glycolytic enzymes lactate:NAD+ oxidoreductase, glyceraldehyde-3-phosphate:NAD+ oxidoreductase, phosphofructokinase, phosphoglucomutase and glucose phosphate isomerase. In contrast, the activity of alpha-glucan phosphorylase was slight. The activity of phosphogluconate:NADP+ oxidoreductase, glucose-6-phosphate:NADP+ oxidoreductase and 5'-nucleotidase was slight, whereas there was no activity of myosin ATPase and mitochondrial ATPase, acid phosphatase or alkaline phosphatase. The high activity of AMP-deaminase was very striking. The activity of peroxidase was moderate. Results obtained with adsorption studies point to adsorption of some of the enzymes studied to the tubular aggregates in vivo and this phenomenon very probably determined the histochemical characteristics of these structures.
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PMID:Histochemical features of tubular aggregates in diseased human skeletal muscle fibres. 317 98

A standard procedure for the identification of the N-terminal amino acid in N alpha-acylated proteins has been developed. After exhaustive proteolysis, the amino acids with blocked alpha-amino groups are separated from positively charged, free amino acids by ion exchange chromatography and subjected to digestion with acylase I. Amino acid analysis before and after the acylase treatment identifies the blocked N-terminal amino acid. A survey of acylamino acid substrates showed that acylase will liberate all the common amino acids except Asp, Cys or Pro from their N-acetyl-and N-butyryl derivatives, and will also catalyze the hydrolysis of N-formyl-Met and N-myristyl-Val. Thus, the procedure cannot identify acylated Asp, Cys or Pro, nor, because of the ion exchange step, N alpha-acyl-derivatives of Arg, Lys or His. Whenever the protease treatment releases free acylamino acids, the remaining amino acids should be detected. When applied to several proteins, the procedure confirmed known N-terminal acylamino acids and identified acyl-Ser in enolases from chum and coho salmon muscle and in pyruvate kinase from rabbit muscle, and acyl-Thr in phosphofructokinase from rabbit muscle. The protease-acylase assay has been used to identify blocked peptides from CNBr- or protease-treated proteins. When such peptides were treated with 1 N HCl at 110 degrees for 10 min, sufficient yields of deacylated, mostly intact, peptide were obtained to permit direct automatic sequencing. The N-terminal sequences of rabbit muscle and coho salmon enolase were determined in this way and are compared to each other and to the sequence of yeast enolase.
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PMID:Studies on N alpha-acylated proteins: the N-terminal sequences of two muscle enolases. 391 71

Normal (line 200) and dystrophic (line 307) embryonic chicken pectoralis muscle cells were studied in cell culture over a period of 2 weeks. During the first 4 days, normal and dystrophic cultures exhibited similar developmental increases in the number of nuclei within multinucleated myotubes, however, dystrophic muscle cells degenerated approximately twice as fast as normal cells once the initial burst of myoblast fusion was complete. The apparent synthesis rate of nonmyofibrillar proteins was similar in normal aand dystrophic cells throughout development, but the apparent synthesis rates of myosin heavy chain and the myofibrillar protein fraction were 50%--90% higher in dystrophic muscle cultures once maturity had been reached (days 6--14). The specific activities of creatine kinase and phosphofructokinase were not affected by the dystrophic condition; however, specific activity of AMP-deaminase was depressed 25%--40% in the dystrophic muscle cultures.
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PMID:Normal and dystrophic embryonic chicken pectoralis muscle cultures: I. Cell differentiation, protein synthesis, and enzyme levels. 645 4

The effect of intermittent high-intensity training on the activity of enzymes involved in purine metabolism and on the concentration of plasma purines following acute short-term intense exercise was investigated. Eleven subjects performed sprint training three times per week for 6 weeks. Muscle biopsies for determination of enzyme activities were obtained prior to and 24 h after the training period. After training, the activity of adenosine 5'-phosphate (AMP) deaminase was lower (P < 0.001) whereas the activities of hypoxanthine phosphoribosyl transferase (HPRT) and phosphofructokinase were significantly higher compared with pre-training levels. The higher activity of HPRT with training suggests an improved potential for rephosphorylation of intracellular hypoxanthine to inosine monophosphate (IMP) in the trained muscle. Before and after the training period the subjects performed four independent 2-min tests at intensities from a mean of 106 to 135% of VO2max. Venous blood was drawn prior to and after each test. The accumulation of plasma hypoxanthine following the four tests was lower following training compared with prior to training (P < 0.05). The accumulation of uric acid was significantly lower (46% of pre-training value) after the test performed at 135% of VO2max (P < 0.05). Based on the observed alterations in muscle enzyme activities and plasma purine accumulation, it is suggested that high intensity intermittent training leads to a lower release of purines from muscle to plasma following intense exercise and, thus, a reduced loss of muscle nucleotides.
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PMID:The effect of high-intensity training on purine metabolism in man. 812 88

A 14-year-old boy with exercise-related myalgia and cramps had several episodes of myoglobinuria since early childhood. An episode at 2 years of age caused acute renal failure. Histochemical and biochemical analysis of muscle showed a combined defect of phosphofructokinase (PFK) and adenosine monophosphate (AMP) deaminase. DNA analysis showed that the patient was homozygous for a G-to-C substitution at codon 39 of the PFK gene (previously described in an Italian patient) and for the common mutation found in AMP deaminase deficiency.
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PMID:Combined defects of muscle phosphofructokinase and AMP deaminase in a child with myoglobinuria. 944

Bacillus sphaericus, a bacterium of biotechnological interest due to its ability to produce mosquitocidal toxins, is unable to use sugars as carbon source. However, ptsHI genes encoding HPr and EI proteins belonging to a PTS were cloned, sequenced and characterized. Both HPr and EI proteins were fully functional for phosphoenolpyruvate-dependent transphosphorylation in complementation assays using extracts from Staphylococcus aureus mutants for one of these proteins. HPr(His(6)) was purified from wild-type and a Ser46/Gln mutant of B. sphaericus, and used for in vitro phosphorylation experiments using extracts from either B. sphaericus or Bacillus subtilis as kinase source. The results showed that both phosphorylated forms, P-Ser46-HPr and P-His15-HPr, could be obtained. The findings also proved indirectly the existence of an HPr kinase activity in B. sphaericus. The genetic structure of these ptsHI genes has some unusual features, as they are co-transcribed with genes encoding metabolic enzymes related to N-acetylglucosamine (GlcNAc) catabolism (nagA, nagB and an undetermined orf2). In fact, this bacterium was able to utilize this amino sugar as carbon and energy source, but a ptsH null mutant had lost this characteristic. Investigation of GlcNAc uptake and streptozotocin inhibition in both a wild-type and a ptsH null mutant strain led to the proposal that GlcNAc is transported and phosphorylated by an EII(Nag) element of the PTS, as yet uncharacterized. In addition, GlcNAc-6-phosphate deacetylase and GlcN-6-phosphate deaminase activities were determined; both were induced in the presence of GlcNAc. These results, together with the authors' recent findings of the presence of a phosphofructokinase activity, are strongly indicative of a glycolytic pathway in B. sphaericus. They also open new possibilities for genetic improvements in industrial applications.
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PMID:Phosphoenolpyruvate phosphotransferase system and N-acetylglucosamine metabolism in Bacillus sphaericus. 1285 20

Effects of exercise on the distribution of phosphofructokinase (PFK), fructose-1,6-biphosphatase (FBPase), and AMP-deaminase between free and particulate-bound fractions was analyzed in white skeletal muscle of rainbow trout Oncorhynchus mykiss. With a widely used technique for the separation of free and bound enzyme fractions (homogenization in low ionic strength, high sucrose buffer), the data showed that the amount of bound PFK increased from 64 to 95% during burst swimming whereas other enzymes were unaffected. Since this data for AMP-deaminase contrasted with earlier reports, different methods of separating free and bound enzyme were evaluated. A clear effect of exercise on AMP-deaminase binding occurred when high ionic strength media (either KCl or KF) were used; in extraction media containing 150 mM KCl, the percent bound rose from 30% in controls to 97% after 1 min burst swimming. Exercise also produced stable changes to AMP-deaminase kinetic properties, including for the bound enzyme (compared with the free) a 2-fold higher Km AMP, a 3-fold higher Ki for inorganic phosphate, and a 60% increase in Ka ADP after 1 min burst exercise. The data suggest that AMP-deaminase in working skeletal muscle is subject to combined controls by allosteric effectors, post-translational modification, and distribution between free and bound states.
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PMID:Influence of exercise on the distribution of enzymes in trout white muscle and kinetic properties of AMP-deaminase from free and bound fractions. 2419 77