Coenzyme B12 Enzymes Part B

Erscheinungsjahr 2022
ISBN: 978-0-323-95557-7
Verlag: William Andrew Publishing

Buch, Englisch, 384 Seiten, Format (B × H): 152 mm x 229 mm, Gewicht: 750 g

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.

Zielgruppe

<p>Biochemists, biophysicists, molecular biologists, analytical chemists, and physiologists</p>

Autoren/Hrsg.

Weitere Mitwirkende

Marsh, Neil

Fachgebiete

• Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)
• Naturwissenschaften Biowissenschaften Molekularbiologie

Inhaltsverzeichnis

B12-dependent radical SAM enzymes 1. Structural characterization of cobalamin-dependent radical SAM methylases Squire Booker Penn State University 2. Purification and characterization of sequential cobalamin-dependent radical SAM methylases ThnK and TokK in -lactam antibiotic biosynthesis Craig Townsend Johns Hopkins University 3. Characterization of the cobalamin-dependent radical S-adenosyl-L-methionine enzyme C-methyltransferase Fom3 in fosfomycin biosynthesis Tadashi Eguchi Tokyo Institute of Technology 4. Studies of OxsB and GenK, two B12-dependent radical SAM enzymes involved in natural product biosynthesis Hung-Wen Liu University of Texas, Austin 5. Purification and structural elucidation of the cobalamin-dependent radical SAM enzyme OxsB Jennifer Bridwell-Rabb University of Michigan

Methods for studying the mechanisms of B12 enzymes 6. Computational investigations of B12-dependent enzymatic reactions Pawel Kozlowski University of Louisville, Kentucky 7. Using kinetic isotope effects to probe the mechanisms of adenosylcobalamin-dependent enzymes Neil Marsh University of Michigan 8. Steady-state and pre-steady state kinetic analysis of ornithine 4,5-aminomutase Kirsten Wolthers University of British Columbia 9. Structural characterization of radical intermediates in reaction of lysine 5,6-aminomutase by EPR, ENDOR, and ESEEM Shyue-Chu Ke National Dong Hwa University, Taiwan 10. Solvent-protein-reaction dynamical coupling in B12 enzyme catalysis Kurt Warncke Emory University, Atlanta 11. Investigating radical pair reaction dynamics of B12 coenzymes using magnetic field effects Alex Jones National Physical Laboratory, U.K. 12. Investigating radical pair reaction dynamics of B12 coenzymes using time-resolved electron paramagnetic resonance spectroscopy Alex Jones National Physical Laboratory, U.K. 13. Time-resolved spectroscopy: Advances in understanding the electronic structure and dynamics of cobalamins Roseanne Sension and James enner-Hahn University of Michigan 14. MCD and Raman Spectroscopy of cobalamin-dependent enzymes Thomas Brunold University of Wisconsin, Madison

Über Autor(innen)

Marsh, Neil
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