Literature DB >> 126584

Activation and inhibition of the Mg-Ca-ATPase from E. coli by Mg2+ and Ca2+.

J Ahlers, T Günther.   

Abstract

MgATP of CaATP is the substrate of the Mg-Ca-ATPase. At low Mg2+- or Ca2+-concentrations the ATPase is activated by Mg2+ or Ca2+, the activator being essential for activity. At higher Mg2+- or Ca2+-concentrations the Mg-Ca-ATPase is inhibited competitively. Thus the real Km is smaller than reported in the literature. H+ competes with Mg2+ or Ca2+ for the metal binding sites.

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Year:  1975        PMID: 126584     DOI: 10.1515/znc-1975-5-618

Source DB:  PubMed          Journal:  Z Naturforsch C Biosci        ISSN: 0341-0382


  3 in total

1.  Kinetic properties of soluble adenosine triphosphatase of Escherichia coli.

Authors:  J Ahlers
Journal:  Mol Cell Biochem       Date:  1977-04-12       Impact factor: 3.396

2.  Partial characterization of the plasma membrane ATPase from a rho0 petite strain of Saccharomyces cerevisiae.

Authors:  J P McDonough; P K Jaynes; H R Mahler
Journal:  J Bioenerg Biomembr       Date:  1980-08       Impact factor: 2.945

3.  Kinetic characterization of plasma membrane ATPase from Saccharomyces cerevisiae.

Authors:  J Ahlers; E Ahr; A Seyfarth
Journal:  Mol Cell Biochem       Date:  1978-11-30       Impact factor: 3.396

  3 in total

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