KEGG   ENZYME: 1.5.8.2
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
Sysname
trimethylamine:electron-transfer flavoprotein oxidoreductase (demethylating)
Reaction(IUBMB)
trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transfer flavoprotein [RN:R02511]
Reaction(KEGG)
R02511
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
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K00317  dimethylamine/trimethylamine dehydrogenase
Genes
PMEXH4W19_11290
RHDR2APBS1_0788
RTHLRK53_05475
DJICH75_07125
DTXATSB10_15590
XBAC7S18_14515
PREPCA10_47330
PFCPflA506_4693(tmd)
POIBOP93_22725
PSHHHU773_024440
TSNW908_00015
THINCRN91_01375
RSORSp0682
RSLRPSI07_mp0583
RSNRSPO_m01017(stcD)
RSMCMR15_mp10652
RSEF504_4539
RSYRSUY_38890(tmd)
RPUCDC45_21030
RSGJK151_04710
COXE0W60_31885
BPHBphy_5960
BCAIK788_0001542
PHSC2L64_21885
PTERC2L65_26085
PSPUNA29_08505
CDNBN940_13011
CFUCFU_2684
CPRACPter91_1920(tmd)
IDCLRM40_18490
MEHM301_1400
MEIMsip34_2459
MEPMPQ_2403
AZAAZKH_p0217
AZIAzCIB_2375
MCIMesci_2636
MOPMesop_5984
MAMMesau_02601
MESWA9K65_014455
MESPC1M53_02585
MERDEB233_12920 EB233_26910
MESRFGU64_14490
AAKAA2016_5993
PHTBLM14_27655
KMNHW532_16390
SMESMa0257
SMKSinme_5357
SMXSM11_pC1602
SMIBN406_04939(tmd)
SMEGC770_GR4pC1294
SMELSM2011_a0257
SMERDU99_24725
SMDSmed_1285
SIXBSY16_2386(hdh) BSY16_277
ATAAWN88_01220
RHIDFFM81_027465
SHZshn_10745 shn_30205
SZOK8M09_09840 K8M09_20940
OINIAR37_22770
OANOant_3262
OAHDR92_3227(hdh)
OPSA8A54_15775
OCHCES85_4558(tmd)
OCRHGK82_18870
OCLGTN27_18995
XAUXaut_0917
STARG3545_26390
LNEFZC33_09600 FZC33_21465
HDNHden_0194 Hden_0535
HDTHYPDE_25228 HYPDE_25748 HYPDE_34963
HMCHYPMC_3962 HYPMC_3963
MCGGL4_2663
BLAGBLTE_16710
PLEOOHA_1_00468(tmd_1) OHA_1_00478(tmd_2)
NOHG5V57_02665 G5V57_05590 G5V57_06430 G5V57_31675
CAULKCG34_05695 KCG34_22905
RUAD1823_18085
RDERD1_4141(tmd)
RLIRLO149_c003340(tmd)
RPONG3256_12605 G3256_12610 G3256_12615
OATOAN307_c42970(tmd)
OAROA238_c47830(tmd1) OA238_c47840(tmd2) OA238_c47850(tmd3)
OTMOSB_15670(tmd)
LMDMETH_21805
LEJETW24_01555 ETW24_05525
YANAYJ57_15570
SUAMBOO69_07220
SULIC1J05_06740 C1J05_19580
SINLDSM14862_03441(tmd_1) DSM14862_03666(tmd_2)
RMMROSMUCSMR3_03636(tmd)
ROKRAK1035_2462
RIDRIdsm_00662(tmd_1) RIdsm_04243(tmd_2) RIdsm_04244(tmd_3)
ROMEI983_01485 EI983_01490 EI983_01495 EI983_09835 EI983_12585
ROHFIU89_18495(tmd)
AHTANTHELSMS3_00564
THAACFI11_03135
MALUKU6B_04850
RHPLPB142_07370
RBLB6K69_00080
PAMNpAMV3p0110(dmd) pAMV3p0194(tmd)
DONBSK21_05955
GEHHYN69_03530 HYN69_12980
GFUKM031_01850 KM031_19465
TAWEI545_11145 EI545_19315
SEDIEBB79_22970 EBB79_23890
HMLHmaOT1_18870
PPRUFDP22_03105
PAEDG5B38_12110 G5B38_17400 G5B38_20470
RBZB9057_07560
NSMJO391_00855 JO391_09270 JO391_14010
SNJA7E77_04570
SMYBJP26_14925
SCHSphch_1857
SMICSmB9_20160
HTQFRZ44_06770 FRZ44_10820 FRZ44_23470 FRZ44_47380
HADHFRZ61_06860 FRZ61_11050 FRZ61_23740
MGOAFA91_30545
MDXBTO20_01230
MDFK0O62_08600
MRFMJO55_07995
MVQMYVA_5919
MMATMMAGJ_23260
MSEIMSEDJ_15750
NYALTV02_09175
RHARHA1_ro01789
ROPROP_14630 ROP_27330
ROAPd630_LPD05948 Pd630_LPD07456
RKOJWS14_09075
GOILK459_16700
TPRTpau_0381
SPHVF9278_41870
SANUK7396_16130
LDNH9L06_06465
NCANoca_0579 Noca_0618
NAROCFH99_14995
PSIMKR76_16005
AGRAAGRA3207_001949
PHHAFB00_19150
PLKCIK06_05545
RRSRoseRS_2964
RCARcas_1934
NAYHYG81_24785
 » show all
Reference
1  [PMID:5116569]
  Authors
Colby J, Zatman LJ.
  Title
The purification and properties of a bacterial trimethylamine dehydrogenase.
  Journal
Biochem J 121:9P-10P (1971)
DOI:10.1042/bj1210009p
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 169:361-9 (1978)
DOI:10.1042/bj1690361
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 270:23958-65 (1995)
DOI:10.1074/jbc.270.41.23958
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 277:8457-65 (2002)
DOI:10.1074/jbc.M111105200
Reference
5  [PMID:11192721]
  Authors
Scrutton NS, Sutcliffe MJ.
  Title
Trimethylamine dehydrogenase and electron transferring flavoprotein.
  Journal
Subcell Biochem 35:145-81 (2000)
DOI:10.1007/0-306-46828-x_5
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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