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:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The release of lipoteichoic acid and mesosomal vesicles to the supernatant buffer during the formation of spherical, osmotically fragile bodies was studied using Streptococcus faecalis ATCC 9790. Autolytic N-acetylmuramidase action was permitted to take place in exponential-phase cells incubated in a buffer which provides an exceptional degree of osmotic stabilization. Both lipoteichoic acid and mesosomal vesicles were relatively rapidly released to the supernatant buffer. Most of the cellular content of lipoteichoic acid (and mesosomal vesicles) was found in the supernatant buffer at incubation times when the cells still retained over 75% of their cell wall. [14-C]- or [3-H]glycerol was used as a label for both cellular lipoteichoic acids and lipid-glycerol. Glycerol in lipoteichoic acid was quantitated after phenol-water and chloroform-methanol treatments and identified by products of acid hydrolysis and its ability to be precipitated by (i) antibodies specific for the polyglycerol-phosphate backbone, (ii) antibodies to the streptococcal group D antigen, and (iii) concanavalin A. Evidence was obtained that lipoteichoic acid was not associated with isolated mesosomal vesicles. Centrifugation of supernates at 200,000 X g sedimented membranous (mesosomal) vesicles and nearly all of the lipid-glycerol present, whereas essentially all of the lipoteichoic acid remained in the supernatant. The sedimented mesosomal vesicles differed from protoplast membrane in their higher lipid-phosphorus to protein ratio and in the absence of detectable levels of two enzymatic activities found in protoplast membranes, adenosine triphosphatase and polynucleotide phosphorylase. Both types of membranes were found to contain DD-carboxypeptidase and LD-transpeptidase activities at nearly the same specific activities. No evidence was obtained for the association of autolytic N-acetylmuramidase activity with either type of membrane preparation.
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PMID:Cellular localization of lipoteichoic acid in Streptococcus faecalis. 80 56

Glycerol (50%, w/w) was found to cause blistering of chick primary myoblast and fibroblast plasma membranes and extensive blistering of 5--6-day-old-myotube plasma plasma membranes in tissue culture. The tips of myoblasts and fibroblasts appeared to be the most sensitive portion of the plasma membrane to the blistering effect of glycerol. The glycerol-induced blistering of myotubes was reduced and delayed by brief EDTA pretreatment. Glycerol treatment (50, 15 and 8% sequentially) of myotubes was used to remove plasma membrane blisters and a plasma membrane-enriched fraction was isolated from these blisters using a modified Dextran T500-polyethylene-glycol 6000 aqueous two-phase polymer system. This fraction was found to be enriched 4.1-fold for 5'-nucleotidase activity, but not for other putative plasma membrane markers, (Na+ + K+)-ATPase activity or alpha-[125I]bungarotoxin binding material. Autoradiographs of alpha-[125I]bungarotoxin, glycerol-treated (50%, w/w) myotubes showed the plasma membrane blisters to be devoid of reduced silver grains. 5'-Nucleotidase was shown to be an ectoenzyme on myoblasts and 5-day-old myotubes and the total cellular activity was present on the cell surface. During the period of myoblast fusion and myotube formation, cell surface activity decreased to a low level while total cellular activity was elevated.
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PMID:Separation of plasma membrane markers by glycerol-induced blistering of muscle cells. 87 40

In glycerol-extracted insect fibrillar muscle suspended in ATP salt solution the incorporation of 32Pi into ATP was studied during the performance of positive or negative oscillatory work and under a variety of mechanical and ionic conditions. An increase in calcium ion concentration from 10(-8)--10(-5) M increased the incorporation rate in proportion to the increase in ATPase activity, mean tension and immediate stiffness, which is a measure of the extent of actin-myosin interaction. Sinusoidal stretches (at 1% Lo) performed at 5 Hz induced the fibres to perform optimal positive oscillatory work and it caused a doubling of the incorporation rate (ant ATPase activity). A decrease or increase of the frequency below or above the optimum of 5 Hz always decreased the power output as well as the incorporation rate which, however, was still noticeable even under conditions where work was done on the fibres. A similar frequency dependence was found when square-wave rather than sinusoidal stretches were applied and this effect could be related to the finding that the rate of stretch-induced incorporation was highest shortly after stretching and then declined to low values (after about 100 ms). These results suggest the formation of an energy-rich intermediate (actomyosin-ADP?) during the contraction process induced by stretching and this intermediate must be assumed to accumulate transiently after stretching.
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PMID:Is the chemomechanical energy transformation reversible? 98 8

Infusions of isotonic or hypertonic (0.3 or 0.5 M) glycerol into the lateral cerebral ventricle (60 min, 0.02 ml/min) of non-hydrated goats invariably induced a conspicuous and sustained water diuresis. Corresponding infusions of 0.3 M glycerol/0.16 M NaCl were almost equally efficient in this respect. A more short-lasting and less pronounced water diuresis was obtained in response to equivalent infusions of pure d-glucose, and the response to 0.3 M glucose/0.16 M NaCl was variable. Intravenous injections of vasopressin blocked the glucose-induced diuresis, but only postponed the glycerol-induced diuresis. Intracerebroventricular (IVT) infusions of 0.5 M glycerol caused a sustained, complete inhibition of the urge to drink in the 48 h dehydrated goat, whereas IVT glucose only attenuated dehydrative drinking. Twenty min after the infusions of glycerol the CSF [Na+] in the lateral ventricle was about 15% below normal. About 10% reduction of CSF [Na+] was obtained 20 min after the IVT infusion of glycerol/NaCl. The corresponding infusion of pure d-glucose reduced the CSF [Na+] by less than 5%. The glycerol and glycerol/NaCl infusions caused a moderate reduction of renal Na+ + K+ excretion. The possibility is discussed that the observed effects of IVT glycerol is a manifestation of its efficiency to inhibit choroidal and/or juxtaventricular (Na+-K+)-ATPase activity.
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PMID:Intracerebroventricular glycerol: a potent inhibitor of ADH-release and thirst. 99 97

We report measurements of the reactivity (degree of labeling, as mole of ligand per mole of protein, at constant exposure time) of the reactive thiol, "SH1", of a subfragment of myosin (S-1), and of Cys-10 of F-actin under various conditions, using N-iodo-[3H]acetyl-N-(1-sulfo-5-naphthyl)ethylenediamine, a fluorescent radioactive iodoacetamide analog. When either ADP or adenyloyl imidodiphosphate (simulating unhydrolyzed ATP) is bound to the enzymatic site of S-1, the reactivity of "SH1" is slightly enhanced, but when active ATPase is going on, reactivity is reduced by about a third, presumably due to the species, (S-1) ADP,Pi. The reactivity of Cys-10 alone is very low. When the complex, (S-1)-F-actin, is formed, the reactivity of SH1 is strongly decreased, and the reactivity of Cys-10 is strongly increased. The foregoing results explain our further observation (on glycerol-treated rabbit psoas fibers) that when fibers labeled in relaxation solution are compared with fibers labeled in rigor solution, myosin is more reactive and actin is less reactive, in the former case; alpha-actinin and C-protein are also less reactive in the former case.
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PMID:Reciprocal reactivities of specific thiols when actin binds to myosin. 106 Nov 33

Differences exist in the coupling of energy to transport of glycine and phenylalanine in aerobically grown cells of Escherichia coli. Energy derived from respiration, although involved in both uptake systems, is not employed identically as shown by kinetic effects of cyanide and anoxia and by temperature dependencies. Additional evidence for aerobic differences was provided by the effects of azide which greatly decreased initial rates of uptake of glycine but not phenylalanine. The effect on glycine uptake was not due to uncoupling of oxidative phosphorylation or to a decrease in respiration rate. Evidence for anaerobic differences was provided by the addition of either glucose or ferricyanide to cell suspensions containing glycerol, thereby maintaining anoxic uptake of phenylalanine, but not glycine, at the aerobic level. Ferricyanide stimulation required a functional Ca, Mg-adenosine 5'-triphosphatase and involved cell metabolism. Ferricyanide was also found to produce differential stimulation of other amino acid transport systems; tyrosine, tryptophan and leucine uptakes were stimulated whereas those for alanine, proline, threonine, and glutamine were relatively unaffected.
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PMID:Differences in coupling of energy to glycine and phenylalanine transport in aerobically grown Escherichia coli. 109 78

In our previous study, we identified four chromatographically distinct DNA-dependent ATPases, B, C1, C2, and C3, in mouse FM3A cells (Tawaragi, Y., Enomoto, T., Watanabe, Y., Hanaoka, F., and Yamada, M. (1984) Biochemistry 23, 529-533). The DNA-dependent ATPase C1 has been purified and characterized in detail. A divalent cation and a polynucleotide cofactor were required for the ATPase activity. Poly(dT), single-stranded circular DNA, and heat-denatured DNA were very effective. Almost no ATPase activity was observed with S1 nuclease-treated native DNA. ATPase C1 hydrolyzed ATP only among the ribo- and deoxyribonucleoside triphosphates tested, and this fact distinguished ATPase C1 from ATPases B, C2, and C3, because the latter enzymes are capable of hydrolyzing both ATP and dATP. The purified DNA-dependent ATPase C1 fraction was shown to have a DNA helicase activity that was dependent on hydrolysis of ATP. The helicase activity and DNA-dependent ATPase activity cosedimented at 5.2 S on glycerol gradient centrifugation. Both activities showed similar preferences for nucleoside 5'-triphosphates and similar requirements for divalent cations. The DNA helicase activity was inhibited by the addition of single-stranded DNAs that served as cofactor for the ATPase activity. The efficiency of a single-stranded DNA to inhibit DNA helicase activity correlated well with the capacity of the DNA to serve as cofactor for DNA-dependent ATPase activity. The helicase was shown to migrate along the DNA strand in the 5' to 3' direction, which is the same direction of migration of the mouse DNA helicase B (Seki, M., Enomoto, T., Yanagisawa, J., Hanaoka, F., and Ui, M. (1988) Biochemistry 27, 1766-1771).
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PMID:DNA-dependent adenosinetriphosphatase C1 from mouse FM3A cells has DNA helicase activity. 131 Sep 78

Cultured ARL15 cells respond to abnormally low extracellular K+ concentrations by increasing the abundance of Na,K-ATPase (the Na/K pump). This response is preceded by significant increases in the mRNAs of the alpha 1 and beta 1 subunits of this enzyme, implying transcriptional or post-transcriptional regulation in the response. The present study concerned the possible participation of serum factors in low K+ induction of Na,K-ATPase. In normal K+ (4.5 mM) or low K+ (0.68 mM) the presence of 10% calf serum had no effect on Na,K-ATPase activity. The serum independence of the response to low K+ raised the possibility that low K+ may itself elicit a "growth" response. Accordingly, the effect of low K+ on mRNA abundances of four proto-oncogenes (c-fos, c-myc, c-jun and c-ski) was evaluated in the early phase of the response by quantitative Northern blot analysis. The mRNA for c-fos was transiently elevated by low K+, with a peak at 30 min. In contrast, low K+ had no measurable effect on the abundances of c-myc, c-jun and c-ski, for up to 2 hr of exposure. The early elevation of c-fos mRNA makes it a candidate mediator in this signal-transduction pathway. Induction of c-fos mRNA by the phorbol ester, PMA, or by dioctanoyl glycerol, however, had no effect on Na,K-ATPase activity. These results indicate that an increase in c-fos mRNA alone is not sufficient to induce Na,K-ATPase. Whether induction of c-fos is necessary for the response to low K+ remains to be determined in future studies.
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PMID:Serum independence of low K+ induction of Na,K-ATPase: possible role of c-fos. 131 15

It is known that two types of high-molecular-mass protease complexes are present in the cytosol of mammalian cells; a 20S latent multicatalytic proteinase named the proteasome, and a large proteolytic complex with an apparent sedimentation coefficient of 26S that catalyzes ATP-dependent breakdown of proteins conjugated with ubiquitin. In this work, we first demonstrated that a low concentration of SDS was required for activation of the latent proteasome, whereas the 26S complex degraded substrates for proteasomes in the absence of SDS. Moreover, the 26S complex was greatly stabilized in the presence of 2 mM ATP and 20% glycerol. Based on these characteristics, we next devised a novel procedure for purification of the 26S proteolytic complexes from human kidney. In this procedure, the proteolytic complexes were precipitated from cytoplasmic extracts by ultracentrifugation for 5 h at 105000 x g, and the large 26S complexes were clearly separated from the 20S proteasomes by molecular-sieve chromatography on a Biogel A-1.5 m column. The 26S enzyme was then purified to apparent homogeneity by successive chromatographies on hydroxyapatite and Q Sepharose, then by glycerol density-gradient centrifugation. Electrophoretic and immunochemical analyses showed that the purified human 26S complex consisted of multiple subunits of proteasomes with molecular masses of 21-31 kDa and 13-15 protein components ranging in molecular mass over 35-110 kDa, which were directly associated with the proteasome. The purified 26S proteolytic complex degraded 125I-labeled lysozyme-ubiquitin conjugates in an ATP-dependent manner. The 26S enzyme also showed high ATPase activity, which was copurified with the complex. Vanadate and hemin strongly inhibited not only ATP cleavage, but also ATP-dependent breakdown of ubiquitinligated proteins, suggesting that the 26S complex hydrolyzes ATP and ubiquitinated proteins by closely linked mechanisms. These findings indicate that the 26S complex consists of a proteasome with proteolytic function and multiple other components including an ATPase that regulates energy-dependent, ubiquitin-mediated protein degradation.
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PMID:Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms. 131 98

We report the purification and characterization of a novel DNA helicase from calf thymus tissue. This enzyme partially copurifies with DNA polymerase epsilon* through many of the chromatographic procedures used to isolate it. The enzyme contains an intrinsic DNA-dependent ATPase activity. It can displace short oligonucleotides annealed to long single stranded substrates, in an ATP-dependent reaction. Use of this assay indicates that the DNA helicase translocates in a 3' to 5' direction with respect to the substrate strand to which it is bound. Maximal efficiency of displacement is accomplished by hydrolysis of (d)ATP as cofactor, however, (d)CTP can also be utilized resulting in a 5-fold decrease in the level of displacement. Displacement activity is enhanced by the presence of saturating amounts of Escherichia coli single stranded DNA-binding protein, not affected by the presence of phage T4 gene 32 protein, and inhibited by human replication factor A. The DNA helicase has a molecular mass of approximately 104 kDa as measured by denaturing gel electrophoresis, and an S value of 5.4 obtained from glycerol gradient sedimentation. Direct [alpha-32P]ATP cross-linking labels a protein of molecular mass approximately 105 kDa, providing further evidence that this polypeptide contains the helicase active site. In view of the differences in the properties of this helicase from four others recently identified in calf and designated A through D, we propose the name helicase E.
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PMID:A novel DNA helicase from calf thymus. 132 24


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