PMID: 8611148Feb 1, 1996Paper

Phospholipid and cation activation of chimaeric choline/ethanolamine phosphotransferases

The Biochemical Journal
C R McMasterR M Bell

Abstract

The Saccharomyces cerevisiae CPT1 and EPT1 genes encode for a cholinephosphotransferase (CPT) and choline/ethanolaminephosphotransferase, respectively. Both Cpt1p and Ept1p activities display an absolute requirement for cations and phospholipids. A mixed-micelle assay was employed to determine cation and lipid activators of parental and chimaeric Cpt1p/Ept1p enzymes to gain insight into their mechanism(s) of activation. Mg2+, Mn2+ and Co2+ were the only cations capable of activating Cpt1p and Ept1p in vitro. Kinetic data revealed that only Mg2+ is present in appropriate amounts to activate CPT activity in vivo. Kinetic data revealed that only Mg2+ is present in appropriate amounts to activate CPT activity in vivo. The two enzymes displayed distinct activation profiles on the basis of their relative affinities for Mg2+, and Mn2+ and Co2+. This allowed the use of chimaeric enzymes to determine the mechanism of cation activation. Cations do not activate Cpt1p or Ept1p by complexing with the substrate, CDP-choline, but instead bind to disparate regions within the enzymes themselves. Cpt1p and Ept1p also displayed distinct phospholipid activation profiles. Phospholipid activation required a phosphate and/or glycero-phosphoester link...Continue Reading

Citations

Jun 17, 2014·The FEBS Journal·Meriyem AktasFranz Narberhaus
Jul 14, 2000·The Journal of Biological Chemistry·A L HenneberryC R McMaster
Nov 25, 1997·Biochimica Et Biophysica Acta·C R McMaster, R M Bell
Dec 3, 1999·Plant Physiology and Biochemistry : PPB·C Miège, É Maréchal
Nov 25, 1997·Biochimica Et Biophysica Acta·C R McMaster, R M Bell

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