Entry
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
ec01120 Microbial metabolism in diverse environments
Orthology
K00317 dimethylamine/trimethylamine dehydrogenase
Genes
MERD : EB233_12920 EB233_26910
MESJ : MJ8_10490 MJ8_44860
SIX : BSY16_2386(hdh) BSY16_277
SZO : K8M09_09840 K8M09_20940
LNE : FZC33_09600 FZC33_21465
HDT : HYPDE_25228 HYPDE_25748 HYPDE_34963
HMC : HYPMC_3962 HYPMC_3963
PLEO : OHA_1_00468(tmd_1) OHA_1_00478(tmd_2)
NOH : G5V57_02665 G5V57_05590 G5V57_06430 G5V57_31675
CAUL : KCG34_05695 KCG34_22905
RPON : G3256_12605 G3256_12610 G3256_12615
RFU : ROLI_013800(tmd_1) ROLI_013810(tmd_2)
OAR : OA238_c47830(tmd1) OA238_c47840(tmd2) OA238_c47850(tmd3)
LEJ : ETW24_01555 ETW24_05525
LCAE : K3721_20240 K3721_20805
SULI : C1J05_06740 C1J05_19580
SINL : DSM14862_03441(tmd_1) DSM14862_03666(tmd_2)
RMM : ROSMUCSMR3_03636(tmd)
RID : RIdsm_00662(tmd_1) RIdsm_04243(tmd_2) RIdsm_04244(tmd_3)
ROM : EI983_01485 EI983_01490 EI983_01495 EI983_09835 EI983_12585
RPEL : N7U68_06485 N7U68_11895
FYT : QF092_00980 QF092_17580 QF092_18440 QF092_19300
PAMN : pAMV3p0110(dmd) pAMV3p0194(tmd)
GEH : HYN69_03530 HYN69_12980
GFU : KM031_01850 KM031_19465
TAW : EI545_11145 EI545_19315
SEDI : EBB79_22970 EBB79_23890
PPSO : QPJ95_18105 QPJ95_18110 QPJ95_19445
PAED : G5B38_12110 G5B38_17400 G5B38_20470
NSM : JO391_00855 JO391_09270 JO391_14010
AMYL : QBD29_02340 QBD29_12395
SLAA : EUU25_06940 EUU25_06985(ndpC)
HTQ : FRZ44_06770 FRZ44_10820 FRZ44_23470 FRZ44_47380
HADH : FRZ61_06860 FRZ61_11050 FRZ61_23740
ROA : Pd630_LPD05948 Pd630_LPD07456
SBAE : DSM104329_00584(tmd_1) DSM104329_02421(tmd_2) DSM104329_02427(tmd_3) DSM104329_03741(tmd_4)
» show all
Taxonomy
Reference
Authors
Colby J, Zatman LJ.
Title
The purification and properties of a bacterial trimethylamine dehydrogenase.
Journal
Reference
Authors
Steenkamp DJ, Singer TP.
Title
Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis.
Journal
Reference
Authors
Huang L, Rohlfs RJ, Hille R.
Title
The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein.
Journal
Reference
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
Reference
Authors
Scrutton NS, Sutcliffe MJ.
Title
Trimethylamine dehydrogenase and electron transferring flavoprotein.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 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
LinkDB
All DBs