1.14.13.148: trimethylamine monooxygenase
This is an abbreviated version!
For detailed information about trimethylamine monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.148
-
1.14.13.148
-
1.14.13.8
-
flavin-containing
-
trimethylamine-n-oxide
-
fad-containing
-
trimethylaminuria
-
methimazole
-
n-oxygenation
-
dimethylaniline
-
s-oxidation
-
n-octylamine
- 1.14.13.148
-
1.14.13.8
-
flavin-containing
- trimethylamine-n-oxide
-
fad-containing
-
trimethylaminuria
- methimazole
-
n-oxygenation
- dimethylaniline
-
s-oxidation
- n-octylamine
Reaction
Synonyms
dimethyl sulfoxide/trimethylamine N-oxide reductase, EC 1.14.13.8, FAD-containing monooxygenase, flavin containing monooxygenase 3, flavin monooxygenase 3, flavin-containing monooxygenase, flavin-containing monooxygenase 3, FMO, FMO3, FMO4, PB7211, TMA monooxygenase, TMA N-oxygenase, TMM
ECTree
Advanced search results
General Information
General Information on EC 1.14.13.148 - trimethylamine monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
malfunction
metabolism
physiological function
-
isozyme FMO3 regulates the conversion of N,N,N-trimethylamine into its N-oxide and hence controls the release of volatile N,N,N-trimethylamine from the individual
-
FMO3 deficiency results in trimethylaminuria or the fish-like odour syndrome
malfunction
-
mutations of the flavin-containing monooxygenase gene FMO3 cause trimethylaminuria
malfunction
trimethylaminuria (fish-odor syndrome) is associated with defective hepatic N-oxidation of dietary-derived trimethylamine catalyzed by flavin-containing monooxygenase
isoform FMO3 in human liver may contribute to the toxicity and/or affect efficacy of ethionamide administration
metabolism
-
the flavin monooxygenase FMO3 contributes to metabolism of anti-tumour triazoloacridinone, C-1305 (5-dimethylaminopropylamino-8-hydroxytriazoloacridinone), in liver microsomes
metabolism
the flavin monooxygenase FMO3 contributes to metabolism of anti-tumour triazoloacridinone, C-1305 (5-dimethylaminopropylamino-8-hydroxytriazoloacridinone), in liver microsomes and Hep-G2 cells
metabolism
the catalytic mechanism comprises a reductive half-reaction and an oxidative half-reaction. In the reductive half-reaction, FAD is reduced by NADPH. In the oxidative half-reaction, the reduced FAD reacts with O2 to form the C4a-(hydro)peroxyflavin