| Type: | Family | Name: | Aminomethyltransferase/Dimethylsulfonioproprionate demethylase DmdA |
| Description: | Dimethlysulfonioproprionate (DMS) is catabolised in marine bacterioplankton through a pathway in which the initial step involves demethylation to methylmercaptopropionate (MMPA), which is then further catabolised to methane thiol and acetate. The enzyme responsible for the first step is dimethylsulfonioproprionate demethylase DmdA [, ].The overall fold of DmdA is not similar to other enzymes that typically utilise the cofactor tetrahydrofolate (THF). Instead DmdA has a triple domain structure similar to that observed for the glycine cleavage T protein []. Glycine cleavage T protein is an aminomethyltransferase which is part of the glycine cleavage complex responsible for the reversible oxidation of glycine [].This entry includes both DmdA and the glycine cleavage T protein. | Short Name: | GCST/DmdA |
