6.2.1.44	additional information	no activity with caprylate and caprate	Ruegeria lacuscaerulensis	?	-	?	89	
6.2.1.44	additional information	no activity with caprylate and caprate	Pseudomonas aeruginosa	?	-	?	89	
6.2.1.44	additional information	no activity with caprylate and caprate	Pseudomonas aeruginosa ATCC 15692	?	-	?	89	
6.2.1.44	additional information	no activity with caprylate and caprate	Candidatus Pelagibacter ubique HTCC1062	?	-	?	89	
6.2.1.44	additional information	no activity with caprylate and caprate	Ruegeria lacuscaerulensis ITI-1157	?	-	?	89	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	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 DmdB, a methylmercaptopropionate-coenzyme A ligase, catalyzes the second step in the demethylation pathway and is a major regulatory point. Two forms of DmdB are present in the marine roseobacter Ruegeria pomeroyi DSS-3, RPO_DmdB1 and RPO_DmdB2	Candidatus Pelagibacter ubique	AMP + diphosphate + 3-(methylthio)propionyl-CoA	-	?	427363	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	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 DmdB, a methylmercaptopropionate-coenzyme A ligase, catalyzes the second step in the demethylation pathway and is a major regulatory point. Two forms of DmdB are present in the marine roseobacter Ruegeria pomeroyi DSS-3, RPO_DmdB1 and RPO_DmdB2	Ruegeria pomeroyi	AMP + diphosphate + 3-(methylthio)propionyl-CoA	-	?	427363	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	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 DmdB, a methylmercaptopropionate-coenzyme A ligase, catalyzes the second step in the demethylation pathway and is a major regulatory point. Two forms of DmdB are present in the marine roseobacter Ruegeria pomeroyi DSS-3, RPO_DmdB1 and RPO_DmdB2	Ruegeria pomeroyi	AMP + diphosphate + 3-methylmercaptopropionyl-CoA	-	?	427364