Paradigm Shift for Radical S-Adenosyl-l-methionine Reactions: The Organometallic Intermediate Ω Is Central to Catalysis-Reference-Cited by-同舟云学术

Paradigm Shift for Radical S-Adenosyl-l-methionine Reactions: The Organometallic Intermediate Ω Is Central to Catalysis

Published:2018-06-28 Issue:28 Volume:140 Page:8634-8638
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Byer Amanda S.¹,Yang Hao²,McDaniel Elizabeth C.¹,Kathiresan Venkatesan²,Impano Stella¹,Pagnier Adrien¹,Watts Hope¹,Denler Carly¹,Vagstad Anna L.³,Piel Jörn³,Duschene Kaitlin S.¹,Shepard Eric M.¹,Shields Thomas P.⁴,Scott Lincoln G.⁴,Lilla Edward A.⁵,Yokoyama Kenichi⁵^ORCID,Broderick William E.¹,Hoffman Brian M.²^ORCID,Broderick Joan B.¹^ORCID

Affiliation:

1. Department of Chemistry & Biochemistry, Montana State University, Bozeman, Montana 59717, United States

2. Department of Chemistry, Northwestern University, Evanston, Illinois 60208, United States

3. Institute of Microbiology, Eidgenössische Technische Hochschule Zürich, Vladimir-Prelog-Weg 4, Zürich 8093, Switzerland

4. Cassia, LLC, 3030 Bunker Hill Street, Ste. 214, San Diego, California 92109, United States

5. Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, United States

Funder

Basic Energy Sciences

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

http://pubs.acs.org/doi/pdf/10.1021/jacs.8b04061

Reference29 articles.

1. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods

2. The Radical SAM Superfamily

3. Radical S-Adenosylmethionine Enzymes

4. Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom. Studies of [2H]glycine-substituted enzyme and peptides homologous to the glycine 734 site.

5. The role of S-adenosylmethionine in the lysine 2,3-aminomutase reaction.

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