The methylthiolation reaction mediated by the Radical-SAM enzymes

Biochim Biophys Acta. 2012 Nov;1824(11):1223-30. doi: 10.1016/j.bbapap.2011.11.007. Epub 2011 Dec 7.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Biocatalysis
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism
  • Free Radicals / chemistry
  • Free Radicals / metabolism
  • Humans
  • Iron-Sulfur Proteins / chemistry
  • Iron-Sulfur Proteins / metabolism*
  • Methyltransferases / chemistry
  • Methyltransferases / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Phylogeny
  • Protein Structure, Tertiary
  • Ribosomal Proteins / chemistry
  • Ribosomal Proteins / metabolism
  • S-Adenosylmethionine / chemistry
  • S-Adenosylmethionine / metabolism*
  • Sulfurtransferases / chemistry
  • Sulfurtransferases / metabolism*

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Free Radicals
  • Iron-Sulfur Proteins
  • Ribosomal Proteins
  • RpsL protein, E coli
  • S-Adenosylmethionine
  • Methyltransferases
  • Sulfurtransferases