Radical S-adenosylmethionine (SAM) enzymes in cofactor biosynthesis: a treasure trove of complex organic radical rearrangement reactions

J Biol Chem. 2015 Feb 13;290(7):3980-6. doi: 10.1074/jbc.R114.623793. Epub 2014 Dec 4.

Abstract

In this minireview, we describe the radical S-adenosylmethionine enzymes involved in the biosynthesis of thiamin, menaquinone, molybdopterin, coenzyme F420, and heme. Our focus is on the remarkably complex organic rearrangements involved, many of which have no precedent in organic or biological chemistry.

Keywords: Biosynthesis; Deazaflavin; Enzyme Mechanism; Heme; Menaquinone; Molybdopterin; Rearrangement; S-Adenosylmethionine (SAM); Thiamin; radical.

Publication types

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

MeSH terms

  • Animals
  • Coenzymes / chemistry
  • Coenzymes / metabolism*
  • Free Radicals / chemistry*
  • Heme / chemistry
  • Heme / metabolism
  • Humans
  • Metalloproteins / chemistry
  • Metalloproteins / metabolism
  • Methylation
  • Molybdenum Cofactors
  • Protein Methyltransferases / metabolism*
  • Pteridines / chemistry
  • Pteridines / metabolism
  • S-Adenosylmethionine / chemistry
  • S-Adenosylmethionine / metabolism*
  • Thiamine / chemistry
  • Thiamine / metabolism
  • Vitamin K 2 / chemistry
  • Vitamin K 2 / metabolism

Substances

  • Coenzymes
  • Free Radicals
  • Metalloproteins
  • Molybdenum Cofactors
  • Pteridines
  • Vitamin K 2
  • Heme
  • S-Adenosylmethionine
  • molybdenum cofactor
  • Protein Methyltransferases
  • Thiamine