Recent advances in HemN-like radical S-adenosyl-l-methionine enzyme-catalyzed reactions

Nat Prod Rep. 2020 Jan 1;37(1):17-28. doi: 10.1039/c9np00032a. Epub 2019 Jul 10.

Abstract

Covering: 2012 to 2019HemN-like radical S-adenosyl-l-methionine (SAM) enzymes have been recently disclosed to catalyze diverse chemically challenging reactions from primary to secondary metabolic pathways. In this highlight, we summarize the reaction examples catalyzed by HemN-like enzymes to date and the enzymatic mechanisms reported. From the recent mechanistic investigations, we reason that there is a shared initiating mechanism wherein a characteristic SAM methylene radical is proposed to abstract a hydrogen atom from an sp3 carbon or add onto an sp2 carbon center although variations occur thereafter from reaction to reaction, as well as providing a brief insight into some future prospects.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Coproporphyrinogen Oxidase / chemistry
  • Coproporphyrinogen Oxidase / metabolism
  • Duocarmycins / metabolism
  • Enzymes / chemistry*
  • Enzymes / metabolism*
  • Escherichia coli Proteins / metabolism
  • Heme / metabolism
  • Hydrogen
  • Methylation
  • Peptides, Cyclic / metabolism
  • Polyketides / metabolism
  • Protein Methyltransferases / metabolism
  • S-Adenosylmethionine / metabolism*
  • Thiazoles / metabolism

Substances

  • Bacterial Proteins
  • Duocarmycins
  • Enzymes
  • Escherichia coli Proteins
  • Peptides, Cyclic
  • Polyketides
  • Thiazoles
  • jawsamycin
  • thiomuracin A
  • yatakemycin
  • Heme
  • CC 1065
  • S-Adenosylmethionine
  • Hydrogen
  • HemN protein, Bacteria
  • Coproporphyrinogen Oxidase
  • ChuW protein, E coli
  • Protein Methyltransferases
  • nosiheptide