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)

ATPase activity and ATP-induced energization of photosynthetic membranes from Rhodopseudomonas capsulata are stimulated by phosphate; the maximum stimulatory effect occurs at a concentration between 1 and 2 mM. The sensitivity of the ATPase to oligomycin increases in the presence of phosphate since all the Pi-stimulated activity is inhibited by this antibiotic. Aurovertin, which has no effect on ATPase in the absence of phosphate, inhibits completely the activity elicited by this anion. The addition of Pi induces a substantial increase in the V of ATPase activity without changing the affinity of the enzyme for ATP or ADP. Arsenate, at the same concentrations, produces effects very similar to those of phosphate. The stimulation by arsenate of the transfer of energy from ATP to the membrane suggests a non-hydrolytic role of this anion as a modifier of the ATPase activity.
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PMID:Energy transduction in photosynthetic bacteria. VIII. Activation of the energy-transducing ATPase by inorganic phosphate. 12 66

1. Study has been made of the effects of a variety of metabolic inhibitors and divalent cations (Ni2+ and Mn2+), normally after 5 min exposure, on the biphasic uptake of inorganic phosphate (Pi) exhibited by phosphate-deprived cells of Escherichia coli, strains AB3311 (Reeves met-) and CBT302 (a (Ca2+ + Mg2+)-ATPase-deficient mutant). 2. In AB3311 cells cyanide (1-10 mM) produced comparable reductions in phosphate uptake to anaerobiosis, but in both instances significant uptake was maintained. Examination of intracellular Pi concentrations showed that, despite these inhibitions, Pi is still concentrated 130 times compared to 394 times under aerobic conditions. Arsenate (100 muM) and iodoacetate (100 muM pre-exposed 15 min) both abolished anaerobic-supported uptake. Under aerobic conditions the former eliminated primary uptake while the latter reduced both phases of uptake 60%. The uncouplers, dinitrophenol (100-1000 muM) and carbonyl cyanide m-chlorophenyl hydrazone (CCCP) (50muM) produced very significant, but not complete inhibitions of both phases of uptake. Inhibitions by iodoacetate and dinitrophenol were additive while dithiothreitol protected against the effects of 50-250 mum CCCP. N,N'-Dicyclo-hexylcarbodiimide (DCCD), the potent inhibitor of membrane-bound (Ca2+ + Mg2+)-ATPase, at 10(-3) M caused significant inhibitions of aerobic- (approx. 60%) and anaerobic- (approx. 80%) supported uptakes thus suggesting some obligatory requirement for this ATPase. 3. CBT302 cells, like AB3311, supported Pi transport both aerobically and anaerobically. CCCP (50muM) reduced the primary uptake similarly to AB3311 cells, but the secondary uptake was less affected. DCCD (10(-5)-10(-3) M), as expected, showed no effects in contrast to AB3311 cells. 4. In AB3311 cells Ni2+ (10 mM) caused significant but different reductions of secondary (70%) and primary (33%) phases of phosphate uptake. Mn2+ (10 mM) showed a greater differential effect with the primary uptake being minimally affected and the secondary uptake being abolished (97%). Partial relief of these inhibitions by Mg2+ (10 mM), suggested that these ions compete with Mg2+ transport. High voltage electrophoresis studies showed that Ni2+ cause intensification in the labelling from 32Pi (i.e. during Pi uptake) of hexose phosphates and a reduction in the labelling of complex molecules left at the origin. With Mn2+, labelling of fructose 1,6-diphosphate was reduced, the triose phosphate area was intensified and an unknown area (X) was intensely labelled. When Mn2+ was combined with anaerobiosis, phosphate uptake though diminished in rate exceeded after 16 min the plateau level of uptake under aerobic conditions with Mn2+ present.
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PMID:Studies on phosphate transport in Escherichia coli. II. Effects of metabolic inhibitors and divalent cations. 13 92

Catalysis by beef heart submitochondrial particles of the medium Pi in equilibrium HOH, Pi in equilibrium ATP, and the ATP in equilibrium HOH exchanges is strongly inhibited while the ATPase and intermediate Pi in equilibrium HOH exchange are accelerated when medium ADP is removed by pyruvate kinase action. Arsenate readily blocks completely the Pi in equilibrium ATP and medium Pi in equilibrium HOH exchange reactions, but not the ATP in equilibrium HOH exchange reaction. The residual ATP in equilibrium HOH exchange in presence of arsenate is inhibited by 2,4-dinitrophenol. These results and other data are explained by an alternating site model for oxidative phosphorylation. In this model during net oxidative phosphorylation ATP is formed at one site but is transitorily tightly bound and not released until ADP and Pi bind at a second site and the membrane ATPase complex is energized. Under conditions of net ATP hydrolysis, ATP binding at one site is accompanied by hydrolysis of the transitorily tightly bound ATP as a second site. Attractive features are only one site of input for conformational energization of the membrane ATPase, a single conformational transition that accounts for both the promotion of ADP and Pi binding in a competent mode and the release of tightly bound ATP, and a symmetry of catalytic sites. The Pi in equilibrium ATP exchange is not inhibited by increase in MgADP and MgATP at constant ratios, and the energy-linked ADP in equilibrium ATP exchange is not inhibited by increased concentrations of MgATP and Pi at a constant ratio. Such exchange patterns indicate a random binding and release of ADP and Pi.
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PMID:An alternating site sequence for oxidative phosphorylation suggested by measurement of substrate binding patterns and exchange reaction inhibitions. 85 91

A. laidlawii membrane vesicles are able to accumulate C14-glucose as well as maltose and fructose against the concentration gradient in the absence of exogeneous entergetic sources. Sugar transport is inhibited by anaerobiosis and by the electron transfer inhibitors such as rotenone and amytal, and by proton conductors such as carbonylcyanide-m-chlorophenylhydrazone. Arsenate and dicyclohexylcarbodimide (inhibitor of membrane-bound ATPase) do not inhibit the sugar transport. It is concluded that sugar transport in the membrane vesicles can be driven by the high-energy state of the membrane or the membrane potential.
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PMID:[Basic evidence for the active transport of carbohydrates in the membrane vesicles of Acholeplasma laidlawii cells]. 86 Dec 65

Regulation of chromosomally determined nutrient cation and anion uptake systems shows important similarities to regulation of plasmid-determined toxic ion resistance systems that mediate the outward transport of deleterious ions. Chromosomally determined transport systems result in accumulation of K+, Mg2+, Fe3+, Mn2+, PO4(3-), SO4(2-), and additional trace nutrients, while bacterial plasmids harbor highly specific resistance systems for AsO2-, AsO4(3-), CrO4(2-), Cd2+, Co2+, Cu2+, Hg2+, Ni2+, SbO2-, TeO3(2-), Zn2+, and other toxic ions. To study the regulation of these systems, we need to define both the trans-acting regulatory proteins and the cis-acting target operator DNA regions for the proteins. The regulation of gene expression for K+ and PO4(3-) transport systems involves two-component sensor-effector pairs of proteins. The first protein responds to an extracellular ionic (or related) signal and then transmits the signal to an intracellular DNA-binding protein. Regulation of Fe3+ transport utilizes the single iron-binding and DNA-binding protein Fur. The MerR regulatory protein for mercury resistance both represses and activates transcription. The ArsR regulatory protein functions as a repressor for the arsenic and antimony(III) efflux system. Although the predicted cadR regulatory gene has not been identified, cadmium, lead, bismuth, zinc, and cobalt induce this system in a carefully regulated manner from a single mRNA start site. The cadA Cd2+ resistance determinant encodes an E1(1)-1E2-class efflux ATPase (consisting of two polypeptides, rather than the one earlier identified). Cadmium resistance is also conferred by the czc system (which confers resistances to zinc and cobalt in Alcaligenes species) via a complex efflux pump consisting of four polypeptides. These two cadmium efflux systems are not otherwise related. For chromate resistance, reduced cellular accumulation is again the resistance mechanism, but the regulatory components are not identified. For other toxic heavy metals (with few exceptions), there exist specific plasmid resistances that remain relatively terra incognita for future exploration of bioinorganic molecular genetics and gene regulation.
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PMID:Gene regulation of plasmid- and chromosome-determined inorganic ion transport in bacteria. 157 10

Arsenate, an analogue of inorganic phosphate, causes an increase in the intrinsic fluorescence of the Ca(2+)-ATPase of sarcoplasmic reticulum membranes. This increase in fluorescence is observed regardless of whether Ca(2+)-loaded or leaky vesicles are assayed. The maximal fluorescence change (2-3%) is observed at pH 6.0 in the presence of Mg2+ and is abolished by the addition of micromolar Ca2+ concentrations. Dimethyl sulfoxide (20% v/v) increases the enzyme's affinity for arsenate one order of magnitude. It is concluded that arsenate, after binding, promotes the same conformational change of the enzyme as that produced by Pi.
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PMID:Arsenate-induced fluorescence changes in the Ca(2+)-ATPase of sarcoplasmic reticulum membranes. 173 24

[Cys374]glutathionyl-actin was prepared by isolation of the reaction product of G-actin with Ellman's reagent (5,5'-dithiobis-(2-nitrobenzoic acid], followed by reaction with glutathione. Filaments of this actin disulfide are susceptible to even weak shearing stress as exerted, for example, by heating to 37 degrees C. This treatment produces a 25-fold enhanced steady-state ATPase activity as compared to unsubstituted F-actin at room temperature. Monitoring the reduction of this enhanced ATPase activity is a reliable method for quantifying the effectiveness of filament-stabilizing agents and for determining their apparent dissociation constants. A detailed comparative study of filament-stabilizing agents was performed, and some hitherto unknown filament-protecting effects were revealed. Inorganic phosphate provides stabilization only to a maximum of 45% ATPase inhibition, but reaches this effect already at cytoplasmic Pi concentrations (approximately 4 mM). Arsenate seems to bind with similar affinity, but with distinctly less protective activity (maximum of 16%). High concentrations of alkali ions provide a more effective protection (maximum of 95%), Li+ being more efficient than Na+ and K+. Divalent cations (Ca2+, Mg2+) had a strong stabilizing effect on KCl-polymerized actin; we confirmed the presence of two distinct classes of binding sites for divalent metal ions with moderate and low affinities, apparent in a strong stabilizing effect on KCl-polymerized actin. The stabilizing effects of KCl and Pi are independent and additive. Correspondingly, at K2HPO4 concentrations greater than 4 mM, K+ ions contribute considerably to stabilization. In the presence of 100 mM KCl plus 4 mM Pi, conditions which mimic the physiological environment, filament protection is nearly as effective as with the mushroom toxin phalloidin. The strong stabilizing effect of phalloidin occurred at concentrations far below stoichiometric, suggesting a very high degree of cooperativity in its interaction with actin filaments.
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PMID:The enhanced ATPase activity of glutathione-substituted actin provides a quantitative approach to filament stabilization. 213 54

Bacterial plasmids have genes that confer highly specific resistances to As, Bi, Cd, Cu, Cr, Hg, Pb, Te, Zn, and other toxic heavy metals. For each toxic cation or anion, generally a different resistance system exists, and these systems may be "linked" together on multiple resistance plasmids. For Cd2+, AsO2-, AsO4(3)-, Hg2+, and organomercurials, DNA sequence analysis has supplemented direct physiological and biochemical experiments to produce sophisticated understanding. The cadA ATPase of S. aureus plasmids is a 727 amino acid membrane ATPase that pumps Cd2+ from the cells as rapidly as it is accumulated. This polypeptide is related by sequence to other cation translocating ATPases, including the membrane K+ ATPases of Escherichia coli and Streptococcus faecalis, the H+ ATPases of yeast and Neurospora, the Na+/K+ ATPases of vertebrate animals, and the Ca2+ ATPases of rabbit muscle. The conserved residues include the aspartyl residue that is phosphorylated, the lysine involved in ATP binding, and the proline within a membrane translocating region. The arsenate and arsenite translocating ATPase consists of 3 polypeptides (from DNA sequence analysis), including a recognizable ATP binding protein (arsA), an integral membrane protein (arsB gene), and a substrate specificity subunit (arsC gene). Inorganic mercury and organomercurial degradation is carried out by a series of about 6 polypeptides, including 2 soluble intracellular enzymes (organomercurial lyase and mercuric reductase). The latter is related by sequence and function to glutathione reductase and lipoamide dehydrogenase of prokaryotes and eukaryotes. These enzymes are dimeric, FAD-containing, NAD(P)H-dependent oxidoreductases. Other recognizable polypeptides in the mer system include a DNA-binding regulatory protein from the merR gene and a Hg2+ transport system consisting of a periplasmic Hg2(+)-binding protein (merP gene) and a membrane protein (merT gene) in gram negative systems.
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PMID:DNA sequence analysis of bacterial toxic heavy metal resistances. 248 81

Bacterial Salmonella enteritidis var. Issatchenko in media without exogenic energy source uptakes K+ in one step with Km 2.1 mM and Vmax 0.08 mM min-1/10(12) cells. This K+ uptake does not depend on pH and osmotic shock and is not inhibited by DCC. Endogenic energy source (glucose) leads to K+ uptake with Km 2.8 mM and Vmax 0.10 mM min-1/10(12) cells, and secretion of H+. The ratio of the DCC-sensitive fluxes of H+ to K+ equals 2. Arsenate and protonophores depress the K+ uptake. Valinomycin decreases the rate of K+ uptake. It is assumed that K+ uptake takes place via the Trk-like system, which works as a separate system as supercomplex with the H+-ATPase complex.
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PMID:[Characteristics of K+ uptake in S. enteritidis bacteria]. 289 51

The effect of arsenate on the partial reactions of the catalytic cycle of the Ca2+ ATPase of skeletal muscle of sarcoplasmic reticulum was studied. With the use of native vesicles it was found that arsenate accelerates the rate of ITP hydrolysis and inhibits both Ca2+ or Sr2+ uptake. These effects were not observed when ATP was used as substrate or, with the use of ITP, when leaky vesicles were assayed. Activation of ITP hydrolysis is related to an increase of the enzyme's apparent affinity for ITP. Arsenate increases the steady-state level of the phosphoenzyme formed from ITP. This depends on the concentration of both Pi and Ca2+, in the medium. Ca2+ and Sr2+ efflux were accelerated by arsenate. The fast Ca2+ efflux promoted by arsenate is impaired by external Ca2+. Arsenate competes with Pi for the phosphorylating site of the enzyme.
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PMID:Effects of arsenate on the Ca2+ ATPase of sarcoplasmic reticulum. 295 98


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