Radical SAM Enzymes

· Methods in Enzymology 606. књига · Academic Press
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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

О аутору

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.

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