Stoichiometry of the Redox Neutral Deamination and Oxidative Dehydrogenation Reactions Catalyzed by the Radical SAM Enzyme DesII-Reference-Cited by-同舟云学术

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

Published:2010-02-01 Issue:7 Volume:132 Page:2359-2369
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Ruszczycky Mark W.¹,Choi Sei-hyun¹,Liu Hung-wen¹

Affiliation:

1. Division of Medicinal Chemistry, College of Pharmacy, and Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, Texas 78712

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja909451a

Reference71 articles.

1. The Radical SAM Superfamily

2. S-Adenosylmethionine: A Wolf in Sheep's Clothing, or a Rich Man's Adenosylcobalamin?

3. 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

4. Spectroscopic Evidence for the Participation of an Allylic Analogue of the 5‘-Deoxyadenosyl Radical in the Reaction of Lysine 2,3-Aminomutase

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

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