KEGG   ENZYME: 1.5.8.2Help
Entry
EC 1.5.8.2                  Enzyme                                 

Name trimethylamine dehydrogenase
Class Oxidoreductases;
Acting on the CH-NH group of donors;
With a flavin as acceptor
BRITE hierarchy
Sysname trimethylamine:electron-transferring flavoprotein oxidoreductase
(demethylating)
Reaction(IUBMB) trimethylamine + H2O + electron-transferring flavoprotein =
dimethylamine + formaldehyde + reduced electron-transferring
flavoprotein [RN:R02511]
Reaction(KEGG) R02511
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Substrate trimethylamine [CPD:C00565];
H2O [CPD:C00001];
electron-transferring flavoprotein [CPD:C04253]
Product dimethylamine [CPD:C00543];
formaldehyde [CPD:C00067];
reduced electron-transferring flavoprotein [CPD:C04570]
Comment A number of alkyl-substituted derivatives of trimethylamine can also
act as electron donors; phenazine methosulfate and
2,6-dichloroindophenol can act as electron acceptors. Contains FAD
and a [4Fe-4S] cluster.
Pathway PATH: ec00680  Methane metabolism
Orthology KO: K00317  trimethylamine dehydrogenase
Genes CAL: CaO19.125(EBP1)
MSU: MS2010(nemA)
BUR: Bcep18194_C7137
RDE: RD1_4141(tmd) RD1_4142(tmd)
SAU: SA0311
SAV: SAV0322
SAM: MW0299
SAR: SAR0319
SAS: SAS0299
SAC: SACOL0392
SAB: SAB0272c
SAA: SAUSA300_0322
SAO: SAOUHSC_00302
SAJ: SaurJH9_0370
SAH: SaurJH1_0381
SAE: NWMN_0315
SHA: SH0268
SPY: SPy_1219
SPZ: M5005_Spy_0933
SPM: spyM18_1171
SPG: SpyM3_0859
SPS: SPs1059
SPJ: MGAS2096_Spy0992
SPF: SpyM50865
SPA: M6_Spy0922
SPB: M28_Spy0905
SAG: SAG1061
SAN: gbs1095
SAK: SAK_1150
MPU: MYPU_7720(baiH)
MMY: MSC_0526
MCP: MCAP_0450
MAA: MAG_0050
Taxonomy
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:5116569]
Colby J, Zatman LJ.
The purification and properties of a bacterial trimethylamine
dehydrogenase.
Biochem. J. 121 (1971) 9P-10P.
Bacterium 4B6
Reference
  Authors
  Title

  Journal
  Organism
2  [PMID:204297]
Steenkamp DJ, Singer TP.
Participation of the iron-sulphur cluster and of the covalently
bound coenzyme of trimethylamine dehydrogenase in catalysis.
Biochem. J. 169 (1978) 361-9.
methylotrophic bacterium
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:7592591]
Huang L, Rohlfs RJ, Hille R.
The reaction of trimethylamine dehydrogenase with electron
transferring flavoprotein.
J. Biol. Chem. 270 (1995) 23958-65.
Methylophilus methylotrophus
Reference
  Authors

  Title

  Journal
  Organism
4  [PMID:11756429]
Jones M, Talfournier F, Bobrov A, Grossmann JG, Vekshin N, Sutcliffe
MJ, Scrutton NS.
Electron transfer and conformational change in complexes of
trimethylamine dehydrogenase and electron transferring flavoprotein.
J. Biol. Chem. 277 (2002) 8457-65.
Methylophilus methylotrophus
Reference
  Authors
  Title
  Journal
5  [PMID:11192721]
Scrutton NS, Sutcliffe MJ.
Trimethylamine dehydrogenase and electron transferring flavoprotein.
Subcell. Biochem. 35 (2000) 145-81.
Other DBs ExplorEnz - The Enzyme Database: 1.5.8.2
IUBMB Enzyme Nomenclature: 1.5.8.2
ExPASy - ENZYME nomenclature database: 1.5.8.2
UM-BBD (Biocatalysis/Biodegradation Database): 1.5.8.2
BRENDA, the Enzyme Database: 1.5.8.2
CAS: 39307-09-0

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