Literature DB >> 6221945

Evaluation of H2O activity in the free or phosphorylated catalytic site of Ca2+-ATPase.

Y Dupont, R Pougeois.   

Abstract

The sarcoplasmic reticulum Ca2+-ATPase catalyses a reversible calcium transport coupled to phosphate transfer between ATP and water. It has been proposed [Biochemistry (1980) 19, 4252-4261] that the reactivity of the acyl-phosphate bond is dependent on the water activity within the catalytic site. We have tested this hypothesis and found that the polarity in the free catalytic site is lower than that of water, a further and large decrease is observed when the enzyme is phosphorylated by Pi. Phosphorylation by ATP indicates that this polarity change is specifically associated with the formation of the ADP-insensitive phosphoenzyme.

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Year:  1983        PMID： 6221945     DOI： 10.1016/0014-5793(83)80255-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  12 in total

1.  Effect of phosphorylation on scallop sarcoplasmic reticulum.

Authors:  P M Hardwicke; J J Bozzola
Journal:  J Muscle Res Cell Motil       Date:  1989-06       Impact factor: 2.698

2.  Formation of the stable structural analog of ADP-sensitive phosphoenzyme of Ca2+-ATPase with occluded Ca2+ by beryllium fluoride: structural changes during phosphorylation and isomerization.

Authors:  Stefania Danko; Takashi Daiho; Kazuo Yamasaki; Xiaoyu Liu; Hiroshi Suzuki
Journal:  J Biol Chem       Date:  2009-06-26       Impact factor: 5.157

Review 3.  Structural basis for E1-E2 conformational transitions in Na,K-pump and Ca-pump proteins.

Authors:  P L Jørgensen; J P Andersen
Journal:  J Membr Biol       Date:  1988-07       Impact factor: 1.843

4.  Direct demonstration of structural changes in soluble, monomeric Ca2+-ATPase associated with Ca2+ release during the transport cycle.

Authors:  J P Andersen; P L Jørgensen; J V Møller
Journal:  Proc Natl Acad Sci U S A       Date:  1985-07       Impact factor: 11.205

5.  Conformational states of sarcoplasmic reticulum Ca2+-ATPase as studied by proteolytic cleavage.

Authors:  J P Andersen; P L Jørgensen
Journal:  J Membr Biol       Date:  1985       Impact factor: 1.843

6.  The mechanism of inhibition of the Ca(2+)-ATPase of skeletal-muscle sarcoplasmic reticulum by the cross-linker o-phthalaldehyde.

Authors:  Y M Khan; A P Starling; J M East; A G Lee
Journal:  Biochem J       Date:  1996-07-15       Impact factor: 3.857

7.  Stimulation of the Ca(2+)-ATPase of sarcoplasmic reticulum by disulfiram.

Authors:  A P Starling; J M East; A G Lee
Journal:  Biochem J       Date:  1996-11-15       Impact factor: 3.857

8.  Increase on the initial soluble heme levels in acidic conditions is an important mechanism for spontaneous heme crystallization in vitro.

Authors:  Renata Stiebler; Anh N Hoang; Timothy J Egan; David W Wright; Marcus F Oliveira
Journal:  PLoS One       Date:  2010-09-13       Impact factor: 3.240

9.  Mechanism of NTP hydrolysis by the Escherichia coli primary replicative helicase DnaB protein. 2. Nucleotide and nucleic acid specificities.

Authors:  Anasuya Roychowdhury; Michal R Szymanski; Maria J Jezewska; Wlodzimierz Bujalowski
Journal:  Biochemistry       Date:  2009-07-28       Impact factor: 3.162

10.  TNP-AMP binding to the sarcoplasmic reticulum Ca(2+)-ATPase studied by infrared spectroscopy.

Authors:  Man Liu; Andreas Barth
Journal:  Biophys J       Date:  2003-11       Impact factor: 4.033
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