The methylthiolation reaction mediated by the Radical-SAM enzymes.

Mohamed Atta (1) , Simon Arragain (1) , Marc Fontecave (1, 2) , Etienne Mulliez (1) , John F Hunt (3) , Jon D Luff , Farhad Forouhar (3)

1 LCBM - UMR 5249 - Laboratoire de Chimie et Biologie des Métaux
2 Collège de France - Chaire Chimie des processus biologiques
3 Department of Biological Sciences [New York]

Over the past 10 years, considerable progress has been made in our understanding of the mechanistic enzymology of the Radical-SAM enzymes. It is now clear that these enzymes appear to be involved in a remarkably wide range of chemically challenging reactions. This review article highlights mechanistic and structural aspects of the methylthiotransferases (MTTases) sub-class of the Radical-SAM enzymes. The mechanism of methylthio insertion, now observed to be performed by three different enzymes is an exciting unsolved problem. This article is part of a Special Issue entitled: Radical SAM enzymes and Radical Enzymology.

Domaines: Chimie inorganique; Sciences du Vivant [q-bio]; Biophysique

Mohamed Atta, Simon Arragain, Marc Fontecave, Etienne Mulliez, John F Hunt, et al.. The methylthiolation reaction mediated by the Radical-SAM enzymes.. BBA - Biochimica et Biophysica Acta, 2012, 1824 (11), pp.1223-30. ⟨10.1016/j.bbapap.2011.11.007⟩. ⟨hal-01073756⟩