Radical SAM Enzymes | Buch | 978-0-12-812794-0 | sack.de

Buch, Englisch, 538 Seiten, Format (B × H): 152 mm x 229 mm, Gewicht: 1110 g

Radical SAM Enzymes


Erscheinungsjahr 2018
ISBN: 978-0-12-812794-0
Verlag: William Andrew Publishing

Buch, Englisch, 538 Seiten, Format (B × H): 152 mm x 229 mm, Gewicht: 1110 g

ISBN: 978-0-12-812794-0
Verlag: William Andrew Publishing


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.
Radical SAM Enzymes jetzt bestellen!

Zielgruppe


<p>The scope of the volume is limited to methods for discovery and biochemistry. The audience is any research who is interested in radical SAM enzymes, or in systems where complex iron-sulfur type metallocenters are required for function.</p>

Weitere Infos & Material


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


Bandarian, Vahe
Vahe Bandarian (b. 1970) received his BS degree in Biochemistry from the California State University in Los Angeles in 1992 working with Scott Grover on kinetic studies of phosphoenolpyruvate carboxylase. He received his PhD in Biochemistry in 1998 from the University of Wisconsin-Madison working under the direction of George Reed carrying out electron paramagnetic studies of the cobalamin-dependent enzyme ethanolamine ammonia-lyase. After carrying out postdoctoral studies with Rowena Matthews on the cobalamin-dependnet methionine synthase at the University of Michigan in Ann Arbor he joined the faculty of the Department of Biochemistry at the University of Arizona in 2003. In 2015 he moved as Professor of Chemistry to the University of Utah. Vahe's lab studies biosynthetic pathways to natural products that include modified nucleic acids and peptides. His contributions have been recognized by a Burroughs Wellcome Career Award in Biomedical Sciences and the Pfizer Award in Enzyme Chemistry by the Division of Biological Chemistry at ACS.


Ihre Fragen, Wünsche oder Anmerkungen
Vorname*
Nachname*
Ihre E-Mail-Adresse*
Kundennr.
Ihre Nachricht*
Lediglich mit * gekennzeichnete Felder sind Pflichtfelder.
Wenn Sie die im Kontaktformular eingegebenen Daten durch Klick auf den nachfolgenden Button übersenden, erklären Sie sich damit einverstanden, dass wir Ihr Angaben für die Beantwortung Ihrer Anfrage verwenden. Selbstverständlich werden Ihre Daten vertraulich behandelt und nicht an Dritte weitergegeben. Sie können der Verwendung Ihrer Daten jederzeit widersprechen. Das Datenhandling bei Sack Fachmedien erklären wir Ihnen in unserer Datenschutzerklärung.