Open AccessS-methyl glutathione synthesis is catalyzed by the cheR methyltransferase in Escherichia coli
Author(s) -
Thomas C. Terwilliger,
Gideon Bollag,
David Sternberg,
Daniel E. Koshland
Publication year - 1986
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.165.3.958-963.1986
Subject(s) - glutathione , escherichia coli , biology , chemotaxis , biochemistry , methyltransferase , gpx6 , glutathione reductase , gpx3 , methylation , receptor , enzyme , glutathione peroxidase , gene
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.