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The specific mechanism of DmdA is still being investigated. However, a mechanism was recently proposed <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 specific mechanism of DmdA is still being investigated. However, a mechanism was recently proposed <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> | ||
| - | [[Image:DmdA_Mechanism.jpg|thumb| | + | [[Image:DmdA_Mechanism.jpg|thumb|700px|left|Proposed mechanism]] |
==Possible Applications== | ==Possible Applications== | ||
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Dimethylsulfoniopropionate-Dependent Demethylase A (DmdA))
IntroductionDimethylsulfoniopropionate-Dependendent Demethylase A (DmdA) is an enzyme produced by marine bacterioplankton in order to demethylate Dimethylsulfoniopropionate (DMSP). StructureThe structure of DmdA was recently solved through X-Ray Diffraction [1]. The structure contains 369 amino acids folded into four domains and containing two ligands. Mechanism of ActionThe specific mechanism of DmdA is still being investigated. However, a mechanism was recently proposed [2] Possible ApplicationsReferences
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