Radical SAM Enzymes, Volume 606

1. Atlas of the Radical SAM Superfamily: Divergent Evolution of Function Using a "Plug and Play" Domain
Gemma L. Holliday, Eyal Akiva, Elaine C. Meng, Shoshana D. Brown, Sara Calhoun, Ursula Pieper, Andrej Sali, Squire J. Booker and Patricia C. Babbitt
2. Purification and Characterization of the Choline Trimethylamine-Lyase (CutC)-Activating Protein CutD
Smaranda Bodea and Emily P. Balskus
3. QueE: A Radical SAM Enzyme Involved in the Biosynthesis of 7-Deazapurine Containing Natural Products
Julia K. Lewis, Nathan A. Bruender and Vahe Bandarian
4. TYW1: A Radical SAM Enzyme Involved in the Biosynthesis of Wybutosine Bases
Anthony P. Young and Vahe Bandarian
5. Mechanistic Studies on the Radical SAM Enzyme Tryptophan Lyase (NosL)
Dhananjay M. Bhandari, Dmytro Fedoseyenko and Tadhg P. Begley
6. Aminofutalosine Synthase (MqnE): A New Catalytic Motif in Radical SAM Enzymology
Sumedh Joshi, Dmytro Fedoseyenko, Nilkamal Mahanta and Tadhg P. Begley
7. Iterative Methylations Resulting in the Biosynthesis of the t-Butyl Group Catalyzed by a B12-Dependent Radical SAM Enzyme in Cystobactamid Biosynthesis
Yuanyou Wang, Bastien Schnell, Rolf Müller and Tadhg P. Begley
8. Biochemical Approaches for Understanding Iron-sulfur Cluster Regeneration in Escherichia coli Lipoyl Synthase during Catalysis
Erin L. McCarthy and Squire J. Booker
9. Using Peptide Mimics to Study the Biosynthesis of the Side-Ring System of Nosiheptide
Bo Wang, Joseph W. LaMattina, Edward D. Badding, Lauren K. Gadsby, Tyler L. Grove and Squire J. Booker
10. Mechanistic Studies of Radical SAM Enzymes: Pyruvate Formate-Lyase Activating Enzyme and Lysine 2,3-Aminomutase Case Studies
Amanda S. Byer, Elizabeth C. McDaniel, Stella Impano, William E. Broderick and Joan B. Broderick
11. Determining Redox Potentials of the Iron–Sulfur Clusters of the AdoMet Radical Enzyme Superfamily
Stephanie J. Maiocco, Lindsey M. Walker and Sean J. Elliott
12. Radical S-Adenosyl-L-Methionine (SAM) Enzyme Involved in the Maturation of the Nitrogenase Cluster
Lee Rettberg, Kazuki Tanifuji, Andrew Jasniewski, Markus Walter Ribbe and Yilin Hu
13. Purification, Characterization, and Biochemical Assays of Biotin Synthase from Escherichia coli
Julia D. Cramer and Joseph T. Jarrett
14. Methods for Expression, Purification, and Characterization of PqqE, a Radical SAM Enzyme in the PQQ Biosynthetic Pathway
Wen Zhu, Ana M. Martins and Judith P. Klinman
15. Methods for Studying the Radical SAM Enzymes in Diphthamide Biosynthesis
Min Dong, Yugang Zhang and Hening Lin
16. Guidelines for Determining the Structures of Radical SAM Enzyme-Catalyzed Modifications in the Biosynthesis of RiPP Natural Products
Leah B. Bushin and Mohammad R. Seyedsayamdost
17. Identification of the Radical SAM Enzymes Involved in the Biosynthesis of Methanopterin and Coenzyme F420 in Methanogens
Kylie D. Allen and Robert H. White
18. Lessons From the Studies of a C-C Bond Forming Radical SAM Enzyme in Molybdenum Cofactor Biosynthesis
Haoran Pang and Kenichi Yokoyama

Radical SAM Enzymes, Volume 606, the latest release in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters on the Characterization of the glycyl radical enzyme choline trimethylamine-lyase and its radical S-adenosylmethionine activating enzyme, Diphathimide biosynthesis, Radical SAM glycyl radical activating enzymes, Radical SAM enzyme BioB in the biosynthesis of biotin, Biogenesis of the PQQ cofactor, Role of MoaAC in the biogenesis of the molybdenum cofactor, Biosynthesis of the nitrogenase cofactor, Bioinformatics of the radical SAM superfamily, The involvement of SAM radical enzymes in the biosynthesis of methanogenic coenzymes, methanopterin and coenzyme F420, and more.

• Provides the authority and expertise of leading contributors from an international board of authors
• Presents the latest release in the Methods in Enzymology series
• Covers radical SAN enzymes in detail

Researchers who are interested in radical SAM enzymes, or in systems where complex iron-sulfur type metallocenters are required for function