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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)

1. The plasma membrane of the flounder erythrocyte contains a Mg2+-dependent ATPase which is insensitive to ouabain. Mg2+ is part of the substrate, Mg-ATP, and Mg2+ also functions as a nonessential activator. 2. Ca2+, Mn2+ and Co2+ can replace Mg2+ as an activator of ATP hydrolysis. Cu2+ and Zn2+ abolish the Mg-dependent activity. It is shown that Ca2+ and Mg2+ activate the same enzyme and that Mg-ATP and Ca-ATP are mutually competitive. 3. The hydrolysis of ATP obeys Michaelis-Menten kinetics whether or not the Mg2+-ATPase is fully activated by Mg2+. The KM values for Mg-ATP were found to be 0.13 and 0.43 mM respectively. 4. Free ATP acts as a competitive inhibitor towards Mg-ATP and the dissociation constant for the enzyme-ATP complex was determined to be about 0.55 mM. 5. The Mg2+ -ATPase has a low specificity and reacts with the common nucleoside triphosphates GTP, ITP, UTP and CTP. 6. The enzyme has a broad pH optimum ranging from 6.5 to 7.2 and an energy of activation of 13.5 kcal/mol between 0 and 30 degrees C. 7. The effect of some activators and inhibitors of membrane-bound ATPases are reported.
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PMID:The Mg2+-dependent ATPase from the erythrocyte plasma membrane of the flounder Platichthys flesus L. General properties and some observations on the steady state kinetics. 613 79

Interaction between Gd3+ and Tb3+ ions and Ca2+,Mg2+-ATPase of sarcoplasmic reticulum was studied. Three classes of lanthanide-ion binding sites with different affinities were distinguished. Binding of Gd3+ to the site with the highest affinity seemed to occur at less than 10(-6)M free Gd3+ and resulted in severe inhibition of ATPase activity. The reaction rates of both E-P formation and decomposition in the forward direction were inhibited in parallel with this binding, whereas ADP-dependent decay of E-P in the backward direction was not. At these Gd3+ concentrations, Ca2+-binding to the transport site was not inhibited. Binding of Gd3+ and Tb3+ to the Ca2+-transport site did occur, but more than 10(-5)M free Gd3+ or Tb3+ was required for effective competition with Ca2+ for that site. Gd3+ bound to the transport site in place of Ca2+ did not activate the E-P intermediate formation. Addition of 10(-1)M Tb3+ to a suspension of sarcoplasmic reticulum membranes resulted in marked enhancement of Tb3+ fluorescence, which is due to an energy transfer from aromatic amino acid residues of ATPase to Tb3+ ions bound to the low affinity site of the enzyme. Gd3+ and Mn2+ competed with Tb3+ for that site, but Ca2+, Zn2+, and Cd2+ did not.
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PMID:Characterization of Gd3+ and Tb3+ binding sites on Ca2+,Mg2+-adenosine triphosphatase of sarcoplasmic reticulum. 614 74

Effects of chlorpromazine, metals and I-ascorbic acid (AA) on Ca2+-ATPase and Mg2+-ATPase in microsomal and granular fractions obtained from the bovine adrenal medulla were studied. Marker enzyme analysis on microsomal subfractions in a discontinuous sucrose density gradient showed a correlation of distribution between ATPase activities and plasma membrane. The two ATPase activities in such plasma membrane-rich microsomes were reduced by chlorpromazine, Hg2+ and Cu2+ (0.3 mM of each), and their effects were greater on the Mg2+-ATPase activity. Zn2+ (0.3 mM) also reduced only the Mg2+-ATPase activity. AA (3 mM) reduced the two ATPase activities to an equal extent. Nevertheless, the inhibitions of ATPases by Hg2+, Cu2+ and Zn2+ were decreased, unaltered and additively enhanced in combination with AA, respectively. We also observed high Mg2+-ATPase activity in the granule-rich fraction, but this ATPase activity was unaffected by all of the above agents. These results indicate that Mg2+-ATPase in the plasma membrane-rich microsome of adrenal medulla is inhibited by chlorpromazine, Hg2+, Cu2+ and Zn2+ more significantly than Ca2+-ATPase, but Mg2+-ATPase in the granular fraction is unaffected, and that AA changes the potency of inhibition by some metals of ATPases diversely.
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PMID:Inhibition by chlorpromazine, metals and I-ascorbic acid of calcium-ATPase and magnesium-ATPase in bovine adrenal medullary microsomes. 614 8

The mechanism of transport of basic amino acids into vacuoles of cells of the yeast Saccharomyces cerevisiae was investigated in vitro. Right-side-out vacuolar membrane vesicles were prepared from purified vacuoles. Arginine was taken up effectively by the vesicles only in the presence of ATP, not in the presence of ADP or AMP-adenosyl-5'-yl imidodiphosphate. It was exchangeable and was released completely by a protonophore, 3,5-di-tert-butyl-4-hydroxybenzilidenemalononitrile (SF6847). The transport required Mg2+ ion but was inhibited by Cu2+, Ca2+, or Zn2+ ions. The transport activity was sensitive to the ATPase inhibitor N,N'-dicyclohexylcarbodiimide (DCCD), but not to oligomycin or sodium vanadate. SF6847 or nigericin blocked arginine uptake completely, but valinomycin had no effect. ATP-dependent formation of a delta pH across the membrane vesicles was shown by quenching of 9-aminoacridine fluorescence. These results indicate that DCCD-sensitive, Mg2+-ATPase of vacuolar membranes is essential as an energy-donating system for the active transport, and that an electrochemical potential difference of protons is a driving force of this basic amino acid transport. Arginine transport showed saturation kinetics with a Km value of 0.6 mM and the mechanism was well explained by an H+/arginine antiport.
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PMID:Active transport of basic amino acids driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae. 645 Jul 64

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

A major mechanism of azole resistance in Candida albicans is overexpression of the genes encoding the ATP binding cassette transporters Cdr1p and Cdr2p due to gain-of-function mutations in Tac1p, a transcription factor of the zinc cluster family. To identify the Tac1p regulon, we analyzed four matched sets of clinical isolates representing the development of CDR1- and CDR2-mediated azole resistance by using gene expression profiling. We identified 31 genes that were consistently up-regulated with CDR1 and CDR2, including TAC1 itself, and 12 consistently down-regulated genes. When a resistant strain deleted for TAC1 was examined similarly, expression of almost all of these genes returned to levels similar to those in the matched azole-susceptible isolate. Using genome-wide location (ChIP-chip) analysis (a procedure combining chromatin immunoprecipitation with hybridization to DNA intergenic microarrays), we found 37 genes whose promoters were bound by Tac1p in vivo, including CDR1 and CDR2. Sequence analysis identified nine new genes whose promoters contain the previously reported Tac1p drug-responsive element (CGGN(4)CGG), including TAC1. In total, there were eight genes whose expression was modulated in the four azole-resistant clinical isolates in a TAC1-dependent manner and whose promoters were bound by Tac1p, qualifying them as direct Tac1p targets: CDR1, CDR2, GPX1 (putative glutathione peroxidase), LCB4 (putative sphingosine kinase), RTA3 (putative phospholipid flippase), and orf19.1887 (putative lipase), as well as IFU5 and orf19.4898 of unknown function. Our results show that Tac1p binds under nonactivating conditions to the promoters of its targets, including to its own promoter. They also suggest roles for Tac1p in regulating lipid metabolism (mobilization and trafficking) and oxidative stress response in C. albicans.
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PMID:Genome-wide expression and location analyses of the Candida albicans Tac1p regulon. 1790 26


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