PMID: 2506093Sep 1, 1989Paper

Heme prosthetic group required for acetylation of prostaglandin H synthase by aspirin

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
Y N Chen, L J Marnett

Abstract

The ability of aspirin to acetylate PGH synthase was determined by reacting [3H-acetyl]-aspirin with purified enzyme followed by high pressure liquid chromatography analysis of the protein components of the reaction mixture. Heme-reconstituted enzyme incorporated approximately one acetyl group per 70-kDa subunit, whereas apoprotein incorporated 0.1 acetyl group per subunit. The ability of the heme prosthetic group to enhance acetylation of the protein was correlated with its ability to protect the Arg253-Gly254 peptide bond from cleavage by trypsin. Thus, heme-induced alteration of protein conformation may contribute to the enhanced labeling of Ser506 by aspirin. The present results indicate that irreversible inactivation of prostaglandin H synthase by aspirin occurs only when the heme prosthetic group is bound to the protein. Considering its short in vivo half-life, it is likely that aspirin inactivates only the steady-state fraction of PGH synthase in a cell that is active but not newly synthesized apoprotein. This may contribute to the differential kinetics of inactivation and recovery of PGH synthase activity in platelets and vascular endothelial cells after administration of low dose aspirin as a prophylactic agent against...Continue Reading

Citations

Jan 31, 2015·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Hezekiel Mathambo KumaloMahmoud E S Soliman
Sep 14, 1989·The New England Journal of Medicine·R YarchoanS Broder
Aug 21, 2013·The Journal of Biological Chemistry·Liang DongWilliam L Smith
May 5, 2001·Plant Science : an International Journal of Experimental Plant Biology·V Ganesan, G Thomas
Apr 24, 1991·Biochimica Et Biophysica Acta·W L Smith, L J Marnett

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