Radical SAM enzymes in methylation and methylthiolation

Structural diversity in the AdoMet radical enzyme superfamily

(2012) Daniel P. Dowling et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Structural Insights into Radical Generation by the Radical SAM Superfamily

(2011) Jessica L. Vey et al.   CHEMICAL REVIEWS

Deficit of tRNALys modification by Cdkal1 causes the development of type 2 diabetes in mice

(2011) Fan-Yan Wei et al.   JOURNAL OF CLINICAL INVESTIGATION

Cfr and RlmN Contain a Single [4Fe-4S] Cluster, which Directs Two Distinct Reactivities forS-Adenosylmethionine: Methyl Transfer by SN2 Displacement and Radical Generation

(2011) Tyler L. Grove et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

RNA methylation by Radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift

(2011) F. Yan et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

A Radically Different Mechanism for S-Adenosylmethionine-Dependent Methyltransferases

(2011) T. L. Grove et al.   SCIENCE

Structural Basis for Methyl Transfer by a Radical SAM Enzyme

(2011) A. K. Boal et al.   SCIENCE

Regioselectivity in the Homolytic Cleavage of S-Adenosylmethionine

(2010) Jack A. Kampmeier   BIOCHEMISTRY

Radical SAM Activation of the B12-Independent Glycerol Dehydratase Results in Formation of 5′-Deoxy-5′-(methylthio)adenosine and Not 5′-Deoxyadenosine

(2010) Jonathan M. Demick et al.   BIOCHEMISTRY

Identification of Eukaryotic and Prokaryotic Methylthiotransferase for Biosynthesis of 2-Methylthio-N6-threonylcarbamoyladenosine in tRNA

(2010) Simon Arragain et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Stoichiometry of the Redox Neutral Deamination and Oxidative Dehydrogenation Reactions Catalyzed by the Radical SAM Enzyme DesII

(2010) Mark W. Ruszczycky et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

RlmN and Cfr are Radical SAM Enzymes Involved in Methylation of Ribosomal RNA

(2010) Feng Yan et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Mechanistic understanding of Pyrococcus horikoshiiDph2, a [4Fe–4S] enzyme required for diphthamidebiosynthesis

(2010) Xuling Zhu et al.   Molecular BioSystems

A radically different enzyme

(2010) Joan B. Broderick   NATURE

Diphthamide biosynthesis requires an organic radical generated by an iron–sulphur enzyme

(2010) Yang Zhang et al.   NATURE

Functional characterization of the YmcB and YqeV tRNA methylthiotransferases of Bacillus subtilis

(2010) Brian P. Anton et al.   NUCLEIC ACIDS RESEARCH

Characterization of RimO, a New Member of the Methylthiotransferase Subclass of the Radical SAM Superfamily

(2009) Kyung-Hoon Lee et al.   BIOCHEMISTRY

Product inhibition in the radicalS-adenosylmethionine family

(2009) Martin R. Challand et al.   FEBS LETTERS

Post-translational Modification of Ribosomal Proteins

(2009) Simon Arragain et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Mechanistic Investigations of Anaerobic Sulfatase-Maturating Enzyme: Direct CβH-Atom Abstraction Catalyzed by a Radical AdoMet Enzyme

(2009) Alhosna Benjdia et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Insights into the structure, function and evolution of the radical-SAM 23S rRNA methyltransferase Cfr that confers antibiotic resistance in bacteria

(2009) Katarzyna H. Kaminska et al.   NUCLEIC ACIDS RESEARCH

Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria

(2009) A. M. B. Giessing et al.   RNA

The Radical SAM Superfamily

(2008) Perry A. Frey et al.   CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY

tRNA's modifications bring order to gene expression

(2008) Estella M Gustilo et al.   CURRENT OPINION IN MICROBIOLOGY

RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli

(2008) B. P. Anton et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme

(2008) J. L. Vey et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA