Add time:08/27/2019         Source:sciencedirect.com

Background: The crystal structure of precorrin-8x methyl mutase (CobH), an enzyme of the aerobic pathway to vitamin B12, provides evidence that the mechanism for methyl migration can plausibly be regarded as an allowed 1, 5-sigmatropic shift of a methyl group from C-11 to C-12 at the C ring of precorrin-8x to afford hydrogenobyrinic acid.Results: The dimeric structure of CobH creates a set of shared active sites that readily discriminate between different tautomers of precorrin-8x and select a discrete tautomer for sigmatropic rearrangement. The active site contains a strictly conserved histidine residue close to the site of methyl migration in ring C of the substrate.Conclusion: Analysis of the structure with bound product suggests that the 1, 5-sigmatropic shift proceeds by protonation of the ring C nitrogen, leading to subsequent methyl migration.

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