title: S-methyl glutathione synthesis is catalyzed by the cheR methyltransferase in Escherichia coli.
abstract: The cheR methyltransferase, known to be necessary for the methyl esterification of receptors involved in chemotaxis, is shown to be essential to the synthesis of S-methyl glutathione from glutathione and S-adenosylmethionine in intact Escherichia coli. S-Methyl glutathione is not, however, found to be essential for chemotaxis. It is suggested that the synthesis of S-methyl glutathione may be due to a "parasitic" reaction of glutathione with S-adenosylmethionine bound to the methyltransferase.
mesh_terms: D002633:Chemotaxis; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism* / Q000502:physiology; D005978:Glutathione / Q000031:analogs & derivatives* / Q000032:analysis / Q000096:biosynthesis / Q000378:metabolism; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism*; D012436:S-Adenosylmethionine / Q000378:metabolism
chemical_list: D012436:S-Adenosylmethionine; D008780:Methyltransferases; C038706:chemotaxis methyltransferase; D005978:Glutathione; C017514:S-methyl glutathione