Following the electrons: peculiarities in the catalytic cycles of radical SAM enzymes

Nat Prod Rep. 2018 Jul 18;35(7):615-621. doi: 10.1039/c7np00058h.

Abstract

Radical SAM enzymes use S-adenosyl-l-methionine as an oxidant to initiate radical-mediated transformations that would otherwise not be possible with Lewis acid/base chemistry alone. These reactions are either redox neutral or oxidative leading to certain expectations regarding the role of SAM as either a reusable cofactor or the ultimate electron acceptor during each turnover. However, these expectations are frequently not realized resulting in fundamental questions regarding the redox handling and movement of electrons associated with these biological catalysts. Herein we provide a focused perspective on several of these questions and associated hypotheses with an emphasis on recently discovered radical SAM enzymes.

Publication types

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

MeSH terms

  • Alkylation
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Carbon-Carbon Lyases / chemistry
  • Carbon-Carbon Lyases / metabolism
  • Carbon-Nitrogen Lyases / chemistry
  • Carbon-Nitrogen Lyases / metabolism
  • Catalysis
  • Enzymes / chemistry*
  • Enzymes / metabolism*
  • Oxidation-Reduction
  • S-Adenosylmethionine / metabolism*

Substances

  • Bacterial Proteins
  • Enzymes
  • LipA protein, Bacteria
  • S-Adenosylmethionine
  • Carbon-Carbon Lyases
  • S-adenosyl-L-methionine tryptophan lyase, Streptomyces actuosus
  • Carbon-Nitrogen Lyases
  • 7-carboxy-7-deazaguanine synthase, Burkholderia multivorans