Coenzyme B12 Enzymes Part B

¡ Methods in Enzymology āĻŦāχ 669 ¡ Academic Press
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āĻāχ āχ-āĻŦ⧁āϕ⧇āϰ āĻŦāĻŋāĻˇā§Ÿā§‡

Coenzyme B12 Enzymes, Part B, Volume 169 in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters on Structural characterization of cobalamin-dependent radical SAM methylases, Purification and characterization of sequential cobalamin-dependent radical SAM methylases ThnK and TokK in -lactam antibiotic biosynthesis, Characterization of the cobalamin-dependent radical S-adenosyl-L-methionine enzyme C-methyltransferase Fom3 in fosfomycin biosynthesis, Studies of OxsB and GenK, two B12-dependent radical SAM enzymes involved in natural product biosynthesis, Purification and structural elucidation of the cobalamin-dependent radical SAM enzyme OxsB, and more. Other chapters discuss Methods for studying the mechanisms of B12 enzymes, Computational investigations of B12 dependent enzymatic reactions, Using kinetic isotope effects to probe the mechanisms of adenosylcobalamin-dependent enzymes, Steady-state and pre-steady state kinetic analysis of ornithine 4,5-aminomutase, and more. - Provides the authority and expertise of leading contributors from an international board of authors - Presents the latest release in Methods in Enzymology series - Includes the latest information on B12 Enzymes

āϞ⧇āĻ–āĻ• āϏāĻŽā§āĻĒāĻ°ā§āϕ⧇

I am currently Professor of Chemistry and Biological Chemistry at the University of Michigan in Ann Arbor. My research interests center on enzyme mechanisms and protein structure and design. We are currently working on a variety of research projects. In particular, we have a long-standing interest in enzymes that use free radicals to catalyze a variety of unusual chemical transformations. More recently, we have become interested in enzymes involved in hydrocarbon biosynthesis, many of which have novel mechanisms and are of practical interest for the biosynthesis of next-generation biofuels. We are also interested in understanding in molecular detail how enzymes interact with abiological surfaces as this is key to many industrial and biomedical applications where enzymes are immobilized on solid supports. More information about my research can be found here:http://www.lsa.umich.edu/chem/people/faculty/ci.marsheneilg_ci.detail

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Neil Marsh āĻāϰ āĻĨ⧇āϕ⧇ āφāϰ⧋

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