EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    6.2.1.44 | more |
no activity with caprylate and caprate |
Ruegeria lacuscaerulensis |
? |
- |
? |
| 6.2.1.44 | more |
no activity with caprylate and caprate |
Pseudomonas aeruginosa |
? |
- |
? |
| 6.2.1.44 | more |
no activity with caprylate and caprate |
Pseudomonas aeruginosa ATCC 15692 |
? |
- |
? |
| 6.2.1.44 | more |
no activity with caprylate and caprate |
Candidatus Pelagibacter ubique HTCC1062 |
? |
- |
? |
| 6.2.1.44 | more |
no activity with caprylate and caprate |
Ruegeria lacuscaerulensis ITI-1157 |
? |
- |
? |
| 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 |
- |
? |
| 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 |
- |
? |
| 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 |
- |
? |
