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Chemistry
and Biochemistry of the
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Related
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The aim of the network is to define the mechanism of enzymatic reactions depending on one of the B12 coenzymes. The attainment of this objective will be possible through the coordinated approach of the partners, which include experts in synthetic organic and bioorganic chemistry, mechanistic and theoretical chemistry, NMR, EPR and X-ray analysis, microbiology, enzymology and molecular biology. Definition of enzymatic mechanism is only possible if the structure of the protein component(s), and where appropriate coenzyme, is known with atomic precision. This requires both crystal structure analyses and, as a complementary exercise, determinations of solution structure. In parallel with structural studies it is important to probe the 'working' enzyme through kinetic and spectroscopic studies. Finally, it is important to attempt to model the proposed enzymatic pathway using both theory and experiment. Several enzyme systems will be studied, ranging from very well characterised (methylmalonyl CoA mutase, glutamate mutase) through less well characterized (ethanolamine ammonia lyase, methyleneglutarate mutase) to novel enzymes (sleeping beautiful mutase). Novel corrinoid enzymes will be identified and characterized from a number of microorganisms (Acetobacterium, Dehalospirillum, Desulfitobacterium).
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| Cost Action D21/0008 Send comments and suggestions about this website to: tmr.b12@ncl.ac.uk |
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