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

Journal of the American Chemical Society ◽

10.1021/ja910850y ◽

2010 ◽

Vol 132 (11) ◽

pp. 3953-3964 ◽

Author(s):

Feng Yan ◽

Jacqueline M. LaMarre ◽

Rene Röhrich ◽

Jochen Wiesner ◽

Hassan Jomaa ◽

...

Keyword(s):

Ribosomal Rna ◽

Radical Sam ◽

Radical Sam Enzymes

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Faculty Opinions recommendation of RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.2647967.2371058 ◽

2010 ◽

Author(s):

Marc Fontecave

Keyword(s):

Ribosomal Rna ◽

Radical Sam ◽

Radical Sam Enzymes

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Faculty Opinions recommendation of RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.2647967.2311068 ◽

2010 ◽

Author(s):

Joan Broderick ◽

Tilak Chandra

Keyword(s):

Ribosomal Rna ◽

Radical Sam ◽

Radical Sam Enzymes

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Faculty Opinions recommendation of RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.2647967.2803054 ◽

2010 ◽

Author(s):

E Neil G Marsh

Keyword(s):

Ribosomal Rna ◽

Radical Sam ◽

Radical Sam Enzymes

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Radical SAM Enzymes

10.1016/s0076-6879(18)x0008-1 ◽

2018 ◽

Keyword(s):

Radical Sam ◽

Radical Sam Enzymes

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Faculty Opinions recommendation of Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1072057.525038 ◽

2007 ◽

Author(s):

Joan Broderick

Keyword(s):

Post Translational Modification ◽

Radical Sam ◽

Radical Sam Enzymes

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Faculty Opinions recommendation of Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.717960468.793471870 ◽

2013 ◽

Author(s):

E Neil G Marsh ◽

Gabriel Román-Meléndez

Keyword(s):

Radical Sam ◽

Radical Sam Enzymes

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Active-Site Controlled, Jahn–Teller Enabled Regioselectivity in Reductive S–C Bond Cleavage of S-Adenosylmethionine in Radical SAM Enzymes

Journal of the American Chemical Society ◽

10.1021/jacs.0c10925 ◽

2020 ◽

Author(s):

Stella Impano ◽

Hao Yang ◽

Richard J. Jodts ◽

Adrien Pagnier ◽

Ryan Swimley ◽

...

Keyword(s):

Active Site ◽

Bond Cleavage ◽

Radical Sam ◽

Radical Sam Enzymes ◽

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Iron–Sulfur Clusters in “Radical SAM” Enzymes: Spectroscopy and Coordination

Metals in Biology - Biological Magnetic Resonance ◽

10.1007/978-1-4419-1139-1_4 ◽

2009 ◽

pp. 53-82 ◽

Author(s):

Serge Gambarelli ◽

Etienne Mulliez ◽

Marc Fontecave

Keyword(s):

Radical Sam ◽

Iron Sulfur Clusters ◽

Radical Sam Enzymes ◽

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H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG

JBIC Journal of Biological Inorganic Chemistry ◽

10.1007/s00775-019-01709-7 ◽

2019 ◽

Vol 24 (6) ◽

pp. 783-792 ◽

Author(s):

Amanda S. Byer ◽

Eric M. Shepard ◽

Michael W. Ratzloff ◽

Jeremiah N. Betz ◽

Paul W. King ◽

...

Keyword(s):

Cluster Assembly ◽

Radical Sam ◽

Radical Sam Enzymes

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Why Nature Uses Radical SAM Enzymes so Widely: Electron Nuclear Double Resonance Studies of Lysine 2,3-Aminomutase Show the 5′-dAdo• “Free Radical” Is Never Free

Journal of the American Chemical Society ◽

10.1021/jacs.5b00498 ◽

2015 ◽

Vol 137 (22) ◽

pp. 7111-7121 ◽

Author(s):

Masaki Horitani ◽

Amanda S. Byer ◽

Krista A. Shisler ◽

Tilak Chandra ◽

Joan B. Broderick ◽

...

Keyword(s):

Free Radical ◽

Double Resonance ◽

Electron Nuclear Double Resonance ◽

Radical Sam ◽

Radical Sam Enzymes

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