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

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

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
Volume1824
Issue number11
DOIs
StatePublished - Nov 2012

Fingerprint

Biosynthesis
Biological Products
Methionine
Enzymes
Transfer RNA
Nucleoside Q
Iron-Sulfur Proteins
Guanosine
Metabolites
Sulfur
Oxidation-Reduction
Proteins
Iron
purine
RNA

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Analytical Chemistry
  • Molecular Biology

Cite this

Radical SAM enzymes involved in the biosynthesis of purine-based natural products. / Bandarian, Vahe.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1824, No. 11, 11.2012, p. 1245-1253.

Research output: Contribution to journalArticle

@article{55aca3f192b44ab3a7cf4d8965235f32,
title = "Radical SAM enzymes involved in the biosynthesis of purine-based natural products",
abstract = "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.",
keywords = "Biosynthesis, Coenzyme F420, Deazapurines, Radical SAM, Wybutosine",
author = "Vahe Bandarian",
year = "2012",
month = "11",
doi = "10.1016/j.bbapap.2012.07.014",
language = "English (US)",
volume = "1824",
pages = "1245--1253",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "11",

}

TY - JOUR

T1 - Radical SAM enzymes involved in the biosynthesis of purine-based natural products

AU - Bandarian, Vahe

PY - 2012/11

Y1 - 2012/11

N2 - 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.

AB - 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.

KW - Biosynthesis

KW - Coenzyme F420

KW - Deazapurines

KW - Radical SAM

KW - Wybutosine

UR - http://www.scopus.com/inward/record.url?scp=84866048164&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84866048164&partnerID=8YFLogxK

U2 - 10.1016/j.bbapap.2012.07.014

DO - 10.1016/j.bbapap.2012.07.014

M3 - Article

C2 - 22902275

AN - SCOPUS:84866048164

VL - 1824

SP - 1245

EP - 1253

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 11

ER -