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. 1986 Mar;165(3):958–963. doi: 10.1128/jb.165.3.958-963.1986

S-methyl glutathione synthesis is catalyzed by the cheR methyltransferase in Escherichia coli.

T C Terwilliger, G E Bollag, D W Sternberg Jr, D E Koshland Jr
PMCID: PMC214522  PMID: 3512532

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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