Methionine sulfoxide formation: the cause of self‐inactivation of reticulocyte lipoxygenase
Open Access
- 3 March 1984
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 139 (3) , 573-576
- https://doi.org/10.1111/j.1432-1033.1984.tb08043.x
Abstract
Under conditions leading to inactivation of reticulocyte lipoxygenase by 13ls-hydroperoxylinoleic acid a single methionine, presumably in the active center of the enzyme, is oxidized to methionine sulfoxide.This publication has 25 references indexed in Scilit:
- The mechanism of inactivation of lipoxygenases by acetylenic fatty acidsEuropean Journal of Biochemistry, 1984
- Self‐Inactivation by 13‐Hydroperoxylinoleic Acid and Lipohydroperoxidase Activity of the Reticulocyte LipoxygenaseEuropean Journal of Biochemistry, 1982
- The biochemistry of methionine sulfoxide residues in proteinsTrends in Biochemical Sciences, 1982
- The Lipoxygenase of ReticulocytesEuropean Journal of Biochemistry, 1979
- Conversion of 9-d- and 13-l-hydroperoxylinoleic acids by soybean lipoxygenase-1 under anaerobic conditionsBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1977
- Evidence for an essential methionine residue in lipoxygenaseFEBS Letters, 1976
- Trivalent copper as a probable intermediate in the reaction catalyzed by galactose oxidaseJournal of the American Chemical Society, 1976
- Reversible alkylation of a methionyl residue near the active site of β-galactosidaseBiochemistry, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Evidence for a Methionyl Residue in the Active Site of the Cytoplasmic Malate Dehydrogenase from Pig HeartHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1969