Sandbox Reserved 497: Difference between revisions
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<ref> Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B., Lanzilotta, W.N. (2012) Structures of dimethylsulfoniopropinate-dependent demethylase from the marine organism pelagabacter ubique. Protein Sci. 21: 289-298. </ref>. The proposed mechanism involves an SN2 intermediate with a concerted methyl and a proton transfer mediated by a water molecule present in the active site. This proposed reaction seems likely due to the location of the active site, which is highly acessible by water, as well as the <scene name='Sandbox_Reserved_497/Acidicactivesite/1'>acidic side chains </scene> present in the active site. Additionally DmdA contains a sulfonium atom which tends to make methyl a fairly good leaving group. | <ref> Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B., Lanzilotta, W.N. (2012) Structures of dimethylsulfoniopropinate-dependent demethylase from the marine organism pelagabacter ubique. Protein Sci. 21: 289-298. </ref>. The proposed mechanism involves an SN2 intermediate with a concerted methyl and a proton transfer mediated by a water molecule present in the active site. This proposed reaction seems likely due to the location of the active site, which is highly acessible by water, as well as the <scene name='Sandbox_Reserved_497/Acidicactivesite/1'>acidic side chains </scene> present in the active site. Additionally DmdA contains a sulfonium atom which tends to make methyl a fairly good leaving group. | ||
[[Image:DmdA_Mechanism.jpg|thumb|550px| | [[Image:DmdA_Mechanism.jpg|thumb|550px|right|The proposed mechanism for the methyl transfer reaction catalyzed by DmdA. This image was obtained directly from Schuller et al.]] | ||
==Possible Applications== | ==Possible Applications== |