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Wiley, Angewandte Chemie International Edition, 21(49), p. 3646-3648, 2010

DOI: 10.1002/anie.201000119

Wiley, Angewandte Chemie, 21(122), p. 3728-3730, 2010

DOI: 10.1002/ange.201000119

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Halomethane Biosynthesis: Structure of a SAM-Dependent Halide Methyltransferase from Arabidopsis thaliana

Journal article published in 2010 by Jason W. Schmidberger, Agata B. James, Robert Edwards, James H. Naismith ORCID, David O'Hagan
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This paper is available in a repository.

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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)