KEGG   ENZYME: 1.14.13.148Help
Entry
EC 1.14.13.148              Enzyme                                 

Name
trimethylamine monooxygenase;
flavin-containing monooxygenase 3;
FMO3;
tmm (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
N,N,N-trimethylamine,NADPH:oxygen oxidoreductase (N-oxide-forming)
Reaction(IUBMB)
N,N,N-trimethylamine + NADPH + H+ + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O [RN:R05623]
Reaction(KEGG)
Substrate
N,N,N-trimethylamine;
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
N,N,N-trimethylamine N-oxide;
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Comment
A flavoprotein. The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy [1,4]. The mammalian enzyme is involved in detoxification of trimethylamine. Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome) [2,3].
History
EC 1.14.13.148 created 2012
Pathway
Methane metabolism
Orthology
K18277  
trimethylamine monooxygenase
Genes
PMY: 
PRE: 
PPG: 
PPUT: 
PPUN: 
PFS: 
PFE: 
PMAN: 
PBA: 
PSV: 
PSK: 
PFZ: 
PPSY: 
PBB: 
PHA: 
PTN: 
MBS: 
MPQ: 
OAI: 
OCE: 
TSN: 
BAV: 
BTRM: 
HAR: 
LCH: 
MEU: 
MXA: 
MLO: 
MCI: 
MOP: 
MAM: 
AAK: 
SME: 
SMK: 
SMQ: 
SMX: 
SMI: 
SMEG: 
SMEL: 
SMER: 
SMD: 
ARA: 
RET: 
REL: 
RLE: 
RLT: 
RLG: 
RLB: 
RLU: 
RTR: 
RHL: 
AZC: 
MSL: 
HMC: 
SIL: 
SPO1551(tmm)
RDE: 
RLI: 
PAMI: 
PSF: 
PSE_p0365(fmo3)
OAR: 
LMD: 
RED: 
CID: 
SSAN: 
GBE: 
GBH: 
GBC: 
GBS: 
GXL: 
PUB: 
APC: 
APM: 
MVA: 
MGI: 
MSP: 
MPHL: 
CGL: 
NCgl1096(Cgl1141)
CGB: 
CGU: 
CGT: 
CGS: 
CGG: 
CGM: 
CGJ: 
CGQ: 
CGX: 
CEF: 
CMD: 
CHM: 
CMQ: 
REQ: 
RPY: 
MIP: 
MVD: 
ARM: 
ARL: 
ARE: 
AAQ: 
ARY: 
ARW: 
PSUL: 
AAI: 
NAL: 
SVI: 
DSL: 
LET: 
TER: 
PSN: 
SHT: 
WVI: 
MYR: 
MPW: 
MOD: 
 » show all
Taxonomy
Reference
1  [PMID:4404764]
  Authors
Large PJ, Boulton CA, Crabbe MJ
  Title
The reduced nicotinamide-adenine dinucleotide phosphate- and oxygen-dependent N-oxygenation of trimethylamine by Pseudomonas aminovorans.
  Journal
Biochem. J. 128 (1972) 137P-138P.
Reference
2  [PMID:9417913]
  Authors
Dolphin CT, Riley JH, Smith RL, Shephard EA, Phillips IR
  Title
Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA.
  Journal
Genomics. 46 (1997) 260-7.
  Sequence
[hsa:2328]
Reference
3  [PMID:9536088]
  Authors
Treacy EP, Akerman BR, Chow LM, Youil R, Bibeau C, Lin J, Bruce AG, Knight M, Danks DM, Cashman JR, Forrest SM
  Title
Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication.
  Journal
Hum. Mol. Genet. 7 (1998) 839-45.
  Sequence
[rno:84493]
Reference
4  [PMID:22006322]
  Authors
Chen Y, Patel NA, Crombie A, Scrivens JH, Murrell JC
  Title
Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 108 (2011) 17791-6.
  Sequence
[msl:Msil_3604]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

DBGET integrated database retrieval system