once released from phytoplankton, marine bacteria degrade dimethylsulfoniopropionate by either the cleavage pathway (to form the volatile gas dimethylsulfide) or the demethylation pathway (yielding methanethiol, which is readily assimilated or oxidized). The enzyme DmdC, 3-(methylthio)propionyl-CoA dehydrogenase, catalyzes the first step in the demethylation pathway
once released from phytoplankton, marine bacteria degrade dimethylsulfoniopropionate by either the cleavage pathway (to form the volatile gas dimethylsulfide) or the demethylation pathway (yielding methanethiol, which is readily assimilated or oxidized). The enzyme DmdC, 3-(methylthio)propionyl-CoA dehydrogenase, catalyzes the first step in the demethylation pathway
a dmdC2 mutant (SPO3804::Tn5) can not grow on 3-(methylthio)propanoate as the sole source of carbon, indicating that this pathway is essential for growth on 3-(methylthio)propanoate. In contrast, the mutant grows similarly to wild-type with 3-(dimethylsulphonio)propanoate, indicating that the cleavage pathway, initiated by DddQ or DddP13, remains capable of supporting growth
in extracts of chemostat-grown cells the levels of DmdB, DmdC and DmdD activities exceed the minimum level, 57 nmol/min*mg of protein, necessary to support growth. The amount of transcripts for dmdB, dmdC and dmdD increase during growth on 3-(methylthio)propanoate or 3-(dimethylsulphonio)propanoate, as expected if the pathway is required for 3-(methylthio)propanoate metabolism
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the amount of transcripts for dmdB, dmdC and dmdD increases during growth of wild-type enzyme on methylmercaptopropionate or 3-(dimethylsulphonio)propanoate, as expected if the pathway is required for 3-(methylthio)propanoate metabolism. Following growth with 3-(dimethylsulphonio)propanoate, the levels of DmdC and DmdD activity in the deletion mutant dmdC are greatly reduced
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1.3.99.B13 3-(methylthio)propionyl-CoA dehydrogenase
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