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:3.6.3.1 (Mg2+-ATPase)
1,484 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A number of ruthenium complexes were tested for their ability to induce filamentation in Escherichia coli. These included monomeric and dimeric complexes with ruthenium in the II or III oxidation states, as well as mixed-valence complexes with ruthenium in the (II,III) oxidation states. In general, dimeric mixed-valence Ru(II,III) complexes were the most active class of compound, although some complexes of this type were relatively inactive. These were pyrazine- or bipyridyl-bridged complexes which are known to involve strong metal-ligand interaction, which stabilizes the Ru(II) oxidation state. Some Ru(III) complexes were also significantly active in induction of filamentous growth in E. coli. One of these was [Ru(NH3)5Cl]Cl2, which did not inhibit electron transport, Mg2+-ATPase activity or DNA synthesis in E. coli, but like [Ru2(NH3)6Br3]Br2 X H2O was a potent inhibitor of respiration-driven calcium transport in the organism. Filament-inducing activity of the complex was reduced in the presence of NaCl, but not in the presence of added Ca2+, ethanol, calcium pantothenate, or E. coli 'division promoting extract'. This behaviour is also similar to that of [Ru2(NH3)6Br3]Br2 X H2O. It is suggested that both complexes may induce filamentation in E. coli by a common mechanism, which may involve interference with calcium metabolism, or a wall or membrane target, rather than interaction with DNA.
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PMID:Filamentation of Escherichia coli K12 elicited by some monomeric, dimeric and trimeric complexes of ruthenium in various oxidation states. 315 89

A water-soluble Mg2+-ATPase previously reported (White, M.D. and Ralston, G.B. (1976) Biochim. Biophys. Acta 436, 567-576) has been purified from human erythrocyte membranes. The purified enzyme has a molecular weight of 575 000; the apparent minimum molecular weight was 100 000, corresponding to a soluble protein of the component 3 region. The Km value for ATP was 1 mM and apparent Km for Mg2+ was 3.6 mM. By means of histochemical activity staining in acrylamide gels it was shown that the purified ATPase preparation could be inhibited by Cd2+ and Zn2+ salts, p-chloromercuribenzoate and N-ethylmaleimide, known inhibitors of membrane endocytosis.
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PMID:Purification of a water-soluble Mg2+-ATPase from human erythrocyte membranes. 610 78

The aim of our work is to show the importance of the role of hydrophobic bonds in maintaining Mg2+-ATPase or sucrase activity and Na+-coupled D-glucose uptake normal for the brush border of rat enterocytes. The activity of the two enzymes and the D-glucose uptake were therefore measured under the action of n-aliphatic alcohols and related to the fluidity determined by ESR. Three concentrations were used for the first eight alcohols, those of octanol being about 1500-times lower than those of methanol. For each alcohol the D-glucose uptake and the fluidity were linear functions of the logarithm of the concentration, the linear regressions being practically parallel and equidistant. The concentrations (C) of the eight alcohols inhibiting the D-glucose uptake by 80% were similar to those increasing the membrane fluidity by 3%. The linear relationship which existed in both cases between log 1/C and log P, P being octanol/water partition coefficients of the alcohols, was evidence of great sensitivity to the hydrophobic effect of the alcohols. Only the first alcohols, however, produced any notable inhibition of Mg2+-ATPase and sucrase. Hydrophobic bonds are thus shown to have little influence in maintaining the activity of Mg2+-ATPase and sucrase, but they modulate the Na+-coupled D-glucose uptake.
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PMID:Sensitivity of Na+-coupled D-glucose uptake, Mg2+-ATPase and sucrase to perturbations of the fluidity of brush-border membrane vesicles induced by n-aliphatic alcohols. 614 7

The effects of tertiary amine local anesthetics (procaine, lidocaine, tetracaine and dibucaine) and chlorpromazine were investigated for three enzyme activities associated with rat brain synaptosomal membranes, i.e., (Na+ + K+)-ATPase (ouabain-sensitive), Mg2+-ATPase (ouabain-insensitive) and acetylcholinesterase. Approximately the same concentrations of each agent gave 50% inhibition of both ATPases, for example 7.9 and 10 mM tetracaine for Mg2+-ATPase and (Na+ + K+)-ATPase, respectively; these concentrations are 10-fold higher than required for inhibition of mitochondrial F1-ATPase. The relative inhibitory potency of the several agents was proportional to their octanol/water partition coefficients. Acetylcholinesterase was inhibited by all agents tested, but the ester anesthetics (procaine and tetracaine) were considerably more potent than the others after correction for partition coefficient differences. For tetracaine, 0.18 mM gave 50% inhibition and showed competitive inhibition on a Lineweaver-Burk plot, but for dibucaine a mixed type of inhibition was observed, and 0.63 mM was required for 50% inhibition. Tetracaine evidently binds at the active site, and dibucaine at the peripheral or modulator site, on this enzyme.
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PMID:Inhibition of synaptosomal enzymes by local anesthetics. 614 63

To determine the effects of graded insulin therapy on cardiac function and biochemistry, rats were made diabetic by streptozotocin (50 mg/kg) and subsequently treated with either 3 U of insulin per day (D3) or 5 U/day (D5) and compared with untreated diabetic rats (D phi) and a nondiabetic control group (C). Blood glucose, water consumption, and heart and body weights in D3 and D5 showed dose-dependent responses between those of D phi and C. Cardiac function was studied at similar heart rates and similar left atrial and aortic pressures in an isolated working heart apparatus. Hearts from D phi showed significant decreases in end-diastolic pressure, peak left ventricular systolic pressure, and positive dP/dt, whereas these values in D3 and D5 were similar to those in C. The isovolumic relaxation period was significantly longer in the D phi group, intermediate between D phi and C in D3, and the same in D5 and C. Ca2+-ATPase activity of myosin and actin-activated Mg2+-ATPase activity was depressed in D phi, partially corrected in D3, and completely corrected in D5. Myosin isoenzyme distribution displayed a shift from the predominant V1 pattern observed in C to a predominant V3 pattern in D phi. Treatment with 3 U of insulin per day partially corrected the isoenzyme abnormality, and treatment with 5 U/day restored the isoenzyme distribution to normal. These results indicate that gross cardiac contractile function can be normalized with insulin dosages that are not sufficient to correct hyperglycemia, polydipsia, or body and heart weight.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of graded insulin therapy on cardiac function in diabetic rats. 623 Sep 40

The content of adenine nucleotides, ATPase activity, the amount of total and inorganic phosphorus in the carp liver mitochondria were studied as affected by CO2 high concentrations. It is shown that during adaptation to the CO2 higher level in the medium the amount of ATP in fishes undergoes the most significant changes. The organism response to the effect of carbon dioxide depends on its concentration in the medium and time of its action. When fishes were for 24h under conditions of the 0.4mM CO2 concentration, the ATP content in the carp liver mitochondria surpasses the control level and under conditions the 0.8 mM CO2 concentration it reaches the control level. The presence of 0.4 and 0.8 mM CO2 concentration decreases the ATP content 7 days later. The amount of inorganic phosphorus in the liver mitochondria of experimental fishes undergoes similar changes. An increase in the CO2 concentration in the water medium up to 0,4 and 0,8 mM inhibits Na+, K+, Mg2+-ATPase in fish organelles, the inhibition being more pronounced in a trial with 0.8 mM CO2.
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PMID:[Peculiarities of phosphoric compound metabolism in liver mitochondria of carp adapted to higher concentrations of CO2 in water]. 624 95

The ATPase activity of purified coupling factor 1 (CF1) of spinach chloroplasts [EC 3.6.1.3] was reversibly enhanced in some aqueous organic solvents, notably methanol, ethanol, and acetone. Pretreatment of CF1 with 20% (v/v) methanol did not affect the subsequent activity. The activity depended entirely on the final concentration of methanol in the reaction mixture. In the presence of 20% methanol, the Km of Ca2+-ATPase from ATP was lowered from 0.4 mM to 0.2 mM. Not only Ca2+, but also Cd2+, Mg2+, Mn2+, and Zn2+ supported the ATPase activity at rates of higher than 7 mumol.mg protein-1 . min-1. Co2+, Ni2+, and Pb2+ supported the activity at rates of 0.5-1.0 mumol.mg protein-1 . min-1. The activities supported by the following cations, if any, were less than 0.2 mumol.mg protein-1 . min-1; Ba2+, Cu2+, Fe2+, Hg2+, Sn2+, and Sr2+. The optimum concentration of methanol for Ca2+-ATPase and Mg2+-ATPase activities was about 30% (v/v). The optimum pH values for Ca2+-ATPase and Mg2+-ATPase activities were about 8.0 and 8.8, respectively. The enhancing effect of organic solvents appears to be associated with their relative lipophilic character as defined by the octanol-water partition coefficient. The Ca2+-ATPase activities of th trypsin-activated and the heat-activated CF1 were inhibited and their Mg2+-ATPase activities were enhanced by the presence of methanol in the reaction mixture.
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PMID:Enhancement of adenosine triphosphatase activity of purified chloroplast coupling factor 1 in aqueous organic solvent. 645 34

The mode of action of dinoseb (2-sec-butyl-4-6-dinitrophenol) on chloroplast reactions was studied. Electron flow from water or from an artificial electron donor, diphenylcarbazide (DPC), to dichlorophenol indophenol (DCPIP) was inhibited at low concentrations of the herbicide (5--10 microM) suggesting a site for dinoseb inhibition at the oxidizing side of photosystem II (PS II). Ferricyanide photoreduction was also inhibited by dinoseb. Cyclic and non-cyclic photophosphorylation and Mg2+-ATPase activity were inhibited by dinoseb, which indicates that this herbicide also acts as an energy transfer inhibitor. Among the above mentioned activities, non-cyclic photophosphorylation was the most sensitive to the inhibition by dinoseb. Ca2+-ATPase activity of solubilized heat activated chloroplast coupling factor 1 (CF1) was stimulated by dinoseb. However, the same activity was inhibited in chloroplasts, which perhaps reflect a difference in the mode of interaction of dinoseb with solubilized and membrane bound coupling factor.
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PMID:Inhibition of electron flow and energy transduction in isolated spinach chloroplasts by the herbicide dinoseb. 742 11

The transbilayer reorientation (flip-flop) of the long-chain amphiphilic anion DENSA (5-(N-decyl)aminonaphthalene-2-sulfonic acid) in the erythrocyte membrane was studied by fluorescence spectroscopy. DENSA intercalates into the membrane at a high membrane/water partition coefficient (3.2.10(5)) and rapidly reorients from the outer to the inner layer in a first order process (k = 0.11 min-1, 37 degrees C, pH 7.4) leading to a steady-state distribution inner:outer layer of about 30:70. The activation energy of the fully reversible and symmetric flip process is about 110 kJ/mol. DIDS and various other established covalent and non-covalent inhibitors of anion transport via the erythrocyte anion exchanger, band 3 (AE 1), suppress the flip to a minimum of about 30-35% of the control. The flip is also inhibited by Cl- with a half maximal inhibitory concentration equal to that required for the inhibition of the exchange flux of ordinary anions via band 3. These findings indicate the involvement of a band 3 mediated (DIDS-sensitive) component of the flip and a DIDS-insensitive one, possibly involving, at least to some extent, simple transbilayer 'diffusion'. This latter component is stimulated by diamide, an SH oxidant known to increase the permeability of the membrane lipid domain of the erythrocyte. Alcohols (butanol, hexanol) accelerate both flip components. Papain treatment, known to inhibit 'ordinary' anion exchange, accelerates both flip and flop. The results suggest that band 3 protein, besides being a conventional transporter of anions, can act as a flippase translocating anionic, membrane-intercalated amphiphiles approaching the transporter from the lipid domain. The flippase mode of operation of band 3 must, however, differ in its mechanism from the conventional exchange mode.
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PMID:Band 3, the anion exchanger of the erythrocyte membrane, is also a flippase. 817 17

The extraordinarily low substrate specificity of P-glycoprotein conflicts with the notion that specific substrate interactions are required in the control of the reaction path in an active transport system. The difficulty is shown to be overcome by a half-coupled mechanism in which the ATP reaction is linked to carrier transformations, as in a fully coupled system, but in which the transported substrate plays a passive role. The mechanism, which requires no specific interaction with the substrate, brings about uphill transport. A half-coupled mechanism is directly supported by two observations: (i) almost completely uncoupled ATPase activity in purified P-glycoprotein, and (ii) a pattern of substrate specificity like that of passive systems, where maximum rates for different substrates vary little (unlike active systems, where maximum rates vary greatly). The mechanism accommodates other findings: partial inhibition of ATPase activity by an actively transported substrate; simultaneous binding and translocation of more than one substrate molecule; and stimulation or inhibition of the transport of one substrate molecule by another. A half-coupled system associated with an internal competitive inhibitor should behave as if tightly coupled, in agreement with the effects of the synthetic peptide, polytryptophan. The degree of coupling in the intact system is yet to be determined, however. A half-coupled ATPase mechanism could originally have evolved in a flippase, where immersion of the carrier in its substrate, the membrane lipid, precludes uncoupled ATP hydrolysis. These concepts may have wider application. An uncoupled antiport mechanism, driven by a proton gradient rather than ATP, can explain low selectivity in the SMR multidrug carriers of bacteria, and a half-coupled mechanism for the ion-driven cotransport of water (the substrate in which the carrier site is immersed) can explain a recently proposed uphill flow of water.
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PMID:Uncoupled active transport mechanisms accounting for low selectivity in multidrug carriers: P-glycoprotein and SMR antiporters. 1055 61


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