Halomethane biosynthesis: Structure of a SAM-dependent halide methyltransferase from arabidopsis thaliana

Jason W. Schmidberger, A.B. B. James, R. Edwards, J.H. H. Naismith, D. O'Hagan

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

It's a gas ! The structure of the halomethane-producing halo/thiocyanate methyltransferase enzyme from plants has been determined. The halide ion and the methyl group of S-adenosyl-L-methionine (SAM) were modeled into the active site (see picture; chloride: green sphere; SAM: C green, O red, S yellow, N blue), which indicated their predisposition for reaction. (Figure Presented) © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.
Original languageEnglish
Pages (from-to)3646-3648
Number of pages3
JournalAngewandte Chemie - International Edition
Volume49
Issue number21
DOIs
Publication statusPublished - 2010

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