Sandbox Reserved 497: Difference between revisions

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==Introduction==
==Introduction==


Dimethylsulfoniproprionate (DMSP) is a common metabolite produced by marine microorganisms and it acts as a significant carbon and sulfur source for marine bacteria. Degradation of DMSP occurs by either the cleavage pathway or the demethylation pathway  <ref> Reisch, C.R., Moran, M.A., Whitman, W.B. (2008). Dimethylsulfoniopropionate-Dependent Demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi. J. Bacteriol. 190: 8018-8024. </ref>. The demethylation pathway is characterized by the conversion of DMSP into methylmercaptopropionate (MMPA). Dimethylsulfoniopropionate-Dependendent Demethylase (DmdA) is the first enzyme in the demethylation pathway and facilitates this conversion by acting as a methyl transferase. In addition to requiring DMSP as a substrate, DmdA also requires (THF) as a cofactor.
Dimethylsulfoniproprionate (DMSP) is a common metabolite produced by marine microorganisms and it acts as a significant carbon and sulfur source for marine bacteria. Degradation of DMSP occurs by either the cleavage pathway or the demethylation pathway  <ref> Reisch, C.R., Moran, M.A., Whitman, W.B. (2008). Dimethylsulfoniopropionate-Dependent Demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi. J. Bacteriol. 190: 8018-8024. </ref>. Understanding both of these degradation pathways is essential due to the key role of DMSP and its degradation product, dimethylsulfide (DMS), in the environmental sulfur cycle <ref>Malin, G. (2006). New Pieces for the Marine Sulfur Cycle Jigsaw. Science. 314: 607-608.</ref>. The demethylation pathway is characterized by the conversion of DMSP into methylmercaptopropionate (MMPA). Recent research has identified dimethylsulfoniopropionate-dependendent demethylase (DmdA) as the inital enzyme in the demethylation pathway. DmdA facilitates this conversion by acting a methyl transferase. While the exact mechanism of demethylation is still unknown, a proposed mechanism has recently been published. Additionally, it is known that DmdA, like many other proteins in its family, requires tetrahydrofolate (THF) as a cofactor.


==Structure==
==Structure==