Role of water in the energy of hydrolysis of phosphate compounds — energy transduction in biological membranes

Meis, Leopoldo de

doi:10.1016/s0005-2728(89)80440-2

Cited by 152 publications

(104 citation statements)

References 127 publications

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“…Hydrophobic Nature of Catalytic Site and Cytoplasmic Domain Organization-Upon formation of E2P from P i in the reverse reaction of its hydrolysis or from ATP in the forward reaction, the atmosphere around the phosphorylation site becomes strongly hydrophobic (15)(16)(17) so that a specific water molecule can attack and hydrolyze the acylphosphate bond. To assess such a nature, the fluorescence of TNP-nucleotide bound to the catalytic site was shown to be very useful as a measure of hydrophobicity (16, 34 -36).…”

Section: Resultsmentioning

confidence: 99%

“…We indicated previously (10 -14) that a large rotation of the A domain (by ϳ90°) and its strong association with the P and N domains most likely occur during the E1P to E2P transition and the Ca 2ϩ release in E2P that has the most compactly organized single headpiece and the hydrophobic atmosphere (5,7,(15)(16)(17) around the phosphorylation site. Our results further suggested that the stabilization energy provided by intimate contacts between the three domains in E2P will provide energy for moving transmembrane helices to open the Ca 2ϩ release pathway to lumen and thus release the bound Ca 2ϩ ions.…”

mentioning

confidence: 76%

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Distinct Natures of Beryllium Fluoride-bound, Aluminum Fluoride-bound, and Magnesium Fluoride-bound Stable Analogues of an ADP-insensitive Phosphoenzyme Intermediate of Sarcoplasmic Reticulum Ca2+-ATPase

Dankó

Yamasaki

Daiho

et al. 2004

Journal of Biological Chemistry

116

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The structural natures of stable analogues for the ADP-insensitive phosphoenzyme (E2P) of Ca 2؉ -ATPase formed in sarcoplasmic reticulum vesicles, i.e. the enzymes with bound beryllium fluoride (BeF⅐E2), bound aluminum fluoride (AlF⅐E2), and bound magnesium fluoride (MgF⅐E2), were explored and compared with those of actual E2P formed from P i without Ca 2؉ . Changes in trinitrophenyl-AMP fluorescence revealed that the catalytic site is strongly hydrophobic in BeF⅐E2 as in E2P but hydrophilic in MgF⅐E2 and AlF⅐E2; yet, the three cytoplasmic domains are compactly organized in these states. Thapsigargin, which was shown in the crystal structure to fix the transmembrane helices and, thus, the postulated Ca 2؉ release pathway to lumen in a closed state, largely reduced the tryptophan fluorescence in BeF⅐E2 as in E2P, but only very slightly (hence, the release pathway is likely closed without thapsigargin) in MgF⅐E2 and AlF⅐E2 as in dephosphorylated enzyme. Consistently, the completely suppressed Ca 2؉ -ATPase activity in BeF-treated vesicles was rapidly restored in the presence of ionophore A23187 but not in its absence by incubation with Ca 2؉ (over several millimolar concentrations) at pH 6, and, therefore, lumenal Ca 2؉ is accessible to reactivate the enzyme. In contrast, no or only very slow restoration was observed with vesicles treated with MgF and AlF even with A23187. BeF⅐E2 thus has the features very similar to those characteristic of the E2P ground state, although AlF⅐E2 and MgF⅐E2 most likely mimic the transition or product state for the E2P hydrolysis, during which the hydrophobic nature around the phosphorylation site is lost and the Ca 2؉ release pathway is closed. The change in hydrophobic nature is probably associated with the change in phosphate geometry from the covalently bound tetrahedral ground state (BeF 3 ؊ ) to trigonal bipyramidal transition state (AlF 3 or AlF 4 ؊ ) and further to tetrahedral product state (MgF 4 2؊ ), and such change likely rearranges transmembrane helices to prevent access and leakage of lumenal Ca 2؉ .Sarcoplasmic reticulum (SR) 1 Ca 2ϩ -ATPase is a representative member of P-type ion-transporting ATPases and catalyzes Ca 2ϩ transport coupled with ATP hydrolysis (Fig. 1) (Refs. 1 and 2 and, for recent reviews, see Refs. 3-6). In the catalytic cycle, the enzyme is activated by the binding of two Ca 2ϩ ions (E2 to Ca 2 E1, steps 1-2) and then autophosphorylated at Asp 351 by MgATP to form ADP-sensitive phosphoenzyme (E1P, steps 3-4). The subsequent isomeric transition to the ADPinsensitive form (E2P) will result in a reduction in affinity, a change in orientation of the Ca 2ϩ binding sites, and Ca 2ϩ release into lumen (steps 5-6). Finally, hydrolysis takes place and returns the enzyme into an unphosphorylated and Ca 2ϩ -unbound form (E2, steps 7-8). E2P can also be formed from P i in the presence of Mg 2ϩ and the absence of Ca 2ϩ by reversal of its hydrolysis, and the subsequent addition of high concentrations of Ca 2ϩ (from the lumenal side) can readily reverse the Ca 2ϩ ...

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 76%

Distinct Natures of Beryllium Fluoride-bound, Aluminum Fluoride-bound, and Magnesium Fluoride-bound Stable Analogues of an ADP-insensitive Phosphoenzyme Intermediate of Sarcoplasmic Reticulum Ca2+-ATPase

Dankó

Yamasaki

Daiho

et al. 2004

Journal of Biological Chemistry

116

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“…cerevisiae ATPase in vesicles, with or without a change in the K , of the enzyme for ATP (Monk et al, 1989). Moreover, data obtained with the Ca2+-ATPase and the Na+/K+-ATPase suggested that the solvent structure at the catalytic site is involved in energy transduction in biological membranes (Meis, 1989). We therefore tried to elucidate the effect on ATPase activity in the crude membrane fraction, extracted from cells grown with or without octanoic acid, of up to 50 mg I-' octanoic acid at pH 6.5 (50 mg acid form, plus 1950 mg octanoate ion 1-l are the expected intracellular concentrations of the two forms based on cytoplasmic accumulation; pHi = 6.5).…”

Section: Eflects Of Octanoic Acid On the Activity Of Plasma Membrane mentioning

confidence: 99%

Activation of plasma membrane ATPase of Saccharomyces cerevisiae by octanoic acid

Viegas

Sá‐Correia²

1991

Journal of General Microbiology

143

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Plasma membrane ATPase activity of Saccharomyces cerettisiae IGC 3507111 grown in the presence of the lipophilic acid octanoic acid I450 mg I-' (0.03435 mM), pH 4.01 was 1-5-fold higher than that in cells grown in its absence. The K,,, for ATP, the pH profile and the sensitivity to orthovanadate of the basal and the activated forms of the membrane ATPase were identical. This activation was closely associated with a decrease in the biomass yield and an increase in the ethanol yield, and was rapidly reversed in uino after removal of the acid. However, the activated level was preserved when membranes were extracted and subjected to manipulations which eliminated or decreased octanoic acid incorporation in the plasma membrane. The activity of the basal plasma membrane ATPase in the total membrane fraction was slightly increased by incubation at pH6.5 with octanoic acid at 100 mg I-' or less (2.4 mg acid form plus 97.6 mg octanoate ion 1-l). However, destruction of the permeability barrier between the enzyme and its substrate could not explain the in tlitfo activation. A role for plasma membrane ATPase activation in the regulation of the intracellular pH (pHi) of cells grown with octanoic acid was not proven.

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“…The energy of hydrolysis of the phosphoanhydride bonds of ATP, pyrophosphate and acyl phosphate residues varies greatly depending on whether these compounds are in solution or bound to the catalytic site of enzymes (for review see [1]). Water activity seems to play a major role in determining the energy of hydrolysis of these compounds [1][2][3][4].…”

Section: Introductionmentioning

confidence: 99%

“…Water activity seems to play a major role in determining the energy of hydrolysis of these compounds [1][2][3][4]. Recently [5] it has been shown for phosphoester bonds such as phosphoserine and glucose phosphate that, different from phosphoanhydride bonds, the energy of hydrolysis does not vary when the water activity of the medium is altered.…”

Section: Introductionmentioning

confidence: 99%

Energy transduction at the catalytic site of enzymes: Hydrolysis of phosphoester bonds and synthesis of pyrophosphate by alkaline phosphatase

Nayudu

Meis

1989

FEBS Letters

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Alkaline phosphatase from mouse intestinal epithelial cells catalyzes the synthesis of pyrophosphate from Pi during hydrolysis of either glucose 6-phosphate, ATP, ADP, inorganic pyrophosphate or p-nitrophenylphosphate. The rate of pyrophosphate synthesis is increased by MgCl 2 and by decreasing the pH of the medium from 8.5 to 6.0. The data presented indicate that at the catalytic site of alkaline phosphatase the energies of hydrolysis of the phosphoserine residue and of pyrophosphate are different from those measured in aqueous solutions.

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Role of water in the energy of hydrolysis of phosphate compounds — energy transduction in biological membranes

Cited by 152 publications

References 127 publications

Distinct Natures of Beryllium Fluoride-bound, Aluminum Fluoride-bound, and Magnesium Fluoride-bound Stable Analogues of an ADP-insensitive Phosphoenzyme Intermediate of Sarcoplasmic Reticulum Ca2+-ATPase

Distinct Natures of Beryllium Fluoride-bound, Aluminum Fluoride-bound, and Magnesium Fluoride-bound Stable Analogues of an ADP-insensitive Phosphoenzyme Intermediate of Sarcoplasmic Reticulum Ca2+-ATPase

Activation of plasma membrane ATPase of Saccharomyces cerevisiae by octanoic acid

Energy transduction at the catalytic site of enzymes: Hydrolysis of phosphoester bonds and synthesis of pyrophosphate by alkaline phosphatase

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