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 or flavoprotein as acceptor
BRITE hierarchy
Sysname
trimethylamine:electron-transfer flavoprotein oxidoreductase (demethylating)
Reaction(IUBMB)
trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transfer flavoprotein [RN:R02511]
Reaction(KEGG)
Substrate
trimethylamine [CPD:C00565];
H2O [CPD:C00001];
electron-transfer flavoprotein [CPD:C04253]
Product
dimethylamine [CPD:C00543];
formaldehyde [CPD:C00067];
reduced electron-transfer 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.
History
EC 1.5.8.2 created 1976 as EC 1.5.99.7, transferred 2002 to EC 1.5.8.2
Pathway
ec00680  Methane metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K00317  dimethylamine/trimethylamine dehydrogenase
Genes
SNJ: A7E77_04570
RHD: R2APBS1_0788
DJI: CH75_07125
DTX: ATSB10_15590
PRE: PCA10_47330
PFC: PflA506_4693(tmd)
POI: BOP93_22725
TSN: W908_00015
RSO: RSp0682
RSL: RPSI07_mp0583
RSN: RSPO_m01017(stcD)
RSE: F504_4539
BPH: Bphy_5960
PSPU: NA29_08505
CFU: CFU_2684
CPRA: CPter91_1920(tmd)
MEH: M301_1400
MEP: MPQ_2403
SME: SMa0257
SMI: BN406_04939(tmd)
SMER: DU99_24725
SMD: Smed_1285
OAN: Oant_3262
OAH: DR92_3227(hdh)
OCH: CES85_4558(tmd)
XAU: Xaut_0917
MCG: GL4_2663
RDE: RD1_4141(tmd)
RLI: RLO149_c003340(tmd)
OAT: OAN307_c42970(tmd)
OAR: OA238_c47830(tmd1) OA238_c47840(tmd2) OA238_c47850(tmd3)
OTM: OSB_15670(tmd)
RMM: ROSMUCSMR3_03636(tmd)
MVQ: MYVA_5919
TPR: Tpau_0381
NCA: Noca_0618
PSIM: KR76_16005
RCA: Rcas_1934
 » show all
Taxonomy
Reference
1  [PMID:5116569]
  Authors
Colby J, Zatman LJ.
  Title
The purification and properties of a bacterial trimethylamine dehydrogenase.
  Journal
Biochem. J. 121 (1971) 9P-10P.
Reference
2  [PMID:204297]
  Authors
Steenkamp DJ, Singer TP.
  Title
Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis.
  Journal
Biochem. J. 169 (1978) 361-9.
Reference
3  [PMID:7592591]
  Authors
Huang L, Rohlfs RJ, Hille R.
  Title
The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein.
  Journal
J. Biol. Chem. 270 (1995) 23958-65.
Reference
4  [PMID:11756429]
  Authors
Jones M, Talfournier F, Bobrov A, Grossmann JG, Vekshin N, Sutcliffe MJ, Scrutton NS.
  Title
Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein.
  Journal
J. Biol. Chem. 277 (2002) 8457-65.
Reference
5  [PMID:11192721]
  Authors
Scrutton NS, Sutcliffe MJ.
  Title
Trimethylamine dehydrogenase and electron transferring flavoprotein.
  Journal
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

DBGET integrated database retrieval system