Coenzyme B12 Enzymes Part B

by Neil Marsh (Editor)

Overview

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

Product Details

ISBN-13:	9780323955584
Publisher:	Elsevier Science & Technology Books
Publication date:	05/27/2022
Series:	Methods in Enzymology , #669
Sold by:	Barnes & Noble
Format:	eBook
Pages:	384
File size:	42 MB
Note:	This product may take a few minutes to download.

About the Author

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

Table of Contents

B12-dependent radical SAM enzymes1. Structural characterization of cobalamin-dependent radical SAM methylasesSquire Booker Penn State University2. Purification and characterization of sequential cobalamin-dependent radical SAM methylases ThnK and TokK in -lactam antibiotic biosynthesisCraig Townsend Johns Hopkins University3. Characterization of the cobalamin-dependent radical S-adenosyl-L-methionine enzyme C-methyltransferase Fom3 in fosfomycin biosynthesisTadashi Eguchi Tokyo Institute of Technology4. Studies of OxsB and GenK, two B12-dependent radical SAM enzymes involved in natural product biosynthesisHung-Wen Liu University of Texas, Austin5. Purification and structural elucidation of the cobalamin-dependent radical SAM enzyme OxsBJennifer Bridwell-Rabb University of Michigan Methods for studying the mechanisms of B12 enzymes6. Computational investigations of B12-dependent enzymatic reactionsPawel Kozlowski University of Louisville, Kentucky7. Using kinetic isotope effects to probe the mechanisms of adenosylcobalamin-dependent enzymesNeil Marsh University of Michigan8. Steady-state and pre-steady state kinetic analysis of ornithine 4,5-aminomutaseKirsten Wolthers University of British Columbia9. Structural characterization of radical intermediates in reaction of lysine 5,6-aminomutase by EPR, ENDOR, and ESEEMShyue-Chu Ke National Dong Hwa University, Taiwan10. Solvent-protein-reaction dynamical coupling in B12 enzyme catalysisKurt Warncke Emory University, Atlanta11. Investigating radical pair reaction dynamics of B12 coenzymes using magnetic field effectsAlex Jones National Physical Laboratory, U.K.12. Investigating radical pair reaction dynamics of B12 coenzymes using time-resolved electron paramagnetic resonance spectroscopyAlex Jones National Physical Laboratory, U.K.13. Time-resolved spectroscopy: Advances in understanding the electronic structure and dynamics of cobalaminsRoseanne Sension and James enner-Hahn University of Michigan14. MCD and Raman Spectroscopy of cobalamin-dependent enzymesThomas Brunold University of Wisconsin, Madison

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From the Publisher

Edited by some of the best scientists in the field, this series presents the latest updates in the field of enzymology