Radical SAM enzymes involved in the biosynthesis of purine-based natural products

Vahe Bandarian

Research output: Contribution to journalReview articlepeer-review

19 Scopus citations


The radical S-adenosyl-l-methionine (SAM) superfamily is a widely distributed group of iron-sulfur containing proteins that exploit the reactivity of the high energy intermediate, 5′-deoxyadenosyl radical, which is produced by the reductive cleavage of SAM, to carry-out complex radical-mediated transformations. The reactions catalyzed by radical SAM enzymes range from simple group migrations to complex reactions in protein and RNA modification. This review will highlight three radical SAM enzymes that catalyze reactions involving modified guanosines in the biosynthesis pathways of the hypermodified tRNA base wybutosine; secondary metabolites of 7-deazapurine structure, including the hypermodified tRNA base queuosine; and the redox cofactor F 420. This article is part of a Special Issue entitled: Radical SAM enzymes and Radical Enzymology.

Original languageEnglish (US)
Pages (from-to)1245-1253
Number of pages9
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Issue number11
StatePublished - Nov 2012


  • Biosynthesis
  • Coenzyme F420
  • Deazapurines
  • Radical SAM
  • Wybutosine

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology


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