Entry
Name
dimethylsulfoniopropionate demethylase;
dmdA (gene name);
dimethylsulfoniopropionate-dependent demethylase A
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S,S-dimethyl-beta-propiothetin:tetrahydrofolate S-methyltransferase
Reaction(IUBMB)
S,S-dimethyl-beta-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate [RN:
R10333 ]
Reaction(KEGG)
Substrate
S,S-dimethyl-beta-propiothetin [CPD:
C04022 ];
tetrahydrofolate [CPD:
C00101 ]
Product
3-(methylsulfanyl)propanoate [CPD:
C08276 ];
5-methyltetrahydrofolate [CPD:
C00440 ]
Comment
The enzyme from the marine bacteria Pelagibacter ubique and Ruegeria pomeroyi are specific towards S,S-dimethyl-beta-propiothetin. They do not demethylate glycine-betaine [1,2].
History
EC 2.1.1.269 created 2013
Pathway
Orthology
K17486 dimethylsulfoniopropionate demethylase
Genes
GAI : IMCC3135_15030(dmdA)
SINL : DSM14862_01560(dmdA)
RMM : ROSMUCSMR3_03150(dmdA)
» show all
Taxonomy
Reference
Authors
Jansen M, Hansen TA
Title
Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria.
Journal
Reference
Authors
Reisch CR, Moran MA, Whitman WB
Title
Dimethylsulfoniopropionate-dependent demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi.
Journal
Sequence
Reference
Authors
Schuller DJ, Reisch CR, Moran MA, Whitman WB, Lanzilotta WN
Title
Structures of dimethylsulfoniopropionate-dependent demethylase from the marine organism Pelagabacter ubique.
Journal
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 2.1.1.269