1.14.13.8: flavin-containing monooxygenase
This is an abbreviated version!
For detailed information about flavin-containing monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.8
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1.14.13.8
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orbit
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methimazole
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trimethylamine
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xenobiotics
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fenna-matthews-olson
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sulfoxide
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n-oxygenation
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excitonic
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s-oxidation
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initio
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bacteriochlorophyll
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frontier
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n-demethylation
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antenna
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tepidum
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drug-metabolizing
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thioureas
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n-octylamine
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phenobarbital
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cdna-expressed
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light-harvesting
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pigment-protein
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imipramine
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metyrapone
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yucca
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chlorobium
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baeyer-villiger
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cyp2c19
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n-hydroxylation
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diels-alder
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hamiltonians
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monooxygenation
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sulfenic
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p-450-dependent
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trimethylamine-n-oxide
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aestuarii
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cyp2a6
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nitrone
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malodor
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hartree-fock
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1-aminobenzotriazole
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ifies
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piperonyl
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drug development
- 1.14.13.8
-
orbit
- methimazole
- trimethylamine
- xenobiotics
-
fenna-matthews-olson
- sulfoxide
-
n-oxygenation
-
excitonic
-
s-oxidation
-
initio
- bacteriochlorophyll
-
frontier
-
n-demethylation
- antenna
- tepidum
-
drug-metabolizing
- thioureas
- n-octylamine
- phenobarbital
-
cdna-expressed
-
light-harvesting
-
pigment-protein
- imipramine
- metyrapone
-
yucca
- chlorobium
-
baeyer-villiger
- cyp2c19
-
n-hydroxylation
-
diels-alder
-
hamiltonians
-
monooxygenation
-
sulfenic
-
p-450-dependent
- trimethylamine-n-oxide
- aestuarii
- cyp2a6
- nitrone
-
malodor
-
hartree-fock
- 1-aminobenzotriazole
-
ifies
-
piperonyl
- drug development
Reaction
Synonyms
class 3 flavin-containing mono-oxygenase, class 3 FMO, dechlorinating flavin-dependent monooxygenase, dimethylaniline monooxygenase (N-oxide-forming), dimethylaniline monooxygenase [N-oxide-forming] 1, dimethylaniline N-oxidase, dimethylaniline oxidase, dimethylsulfone monooxygenase, DMA oxidase, EC 1.13.12.11, EC 1.8.1.3, EtaA, FAD-containing monooxygenase, FAD-containing monooxygenase 3, flavin containing monooxygenase 3, flavin mono-oxygenase, flavin monooxygenase, flavin-containing mono-oxygenase, flavin-containing monooxygenase, flavin-containing monooxygenase 1, flavin-containing monooxygenase 3, flavin-containing monooxygenase 5, flavin-containing monooxygenase-3, flavin-containing-monooxygenase, flavin-dependent monooxygenase, flavoprotein monooxygenase, FMO, FMO 1A1, FMO 1B1, FMO 1C1, FMO 1D1, FMO 1E1, FMO-E, FMO-I, FMO-II, FMO1, FMO2, FMO2.1, FMO3, FMO4, FMO5, FMOGS-OX6, FMOGS-OX7, HadA, hFMO1, hFMO3, hFMO5, Met S-oxidase, mFMO, mixed-function amine oxidase, monooxygenase FMO1, More, MymA, N,N-dimethylaniline monooxygenase, oxygenase, dimethylaniline mono- (N-oxide-forming), oxygenase, methylphenyltetrahydropyridine N-mono-, PtFMO, sfnG, TetX, type II flavin-containing monooxygenase
ECTree
1.14.13.8 flavin-containing monooxygenaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 1.14.13.8 - flavin-containing monooxygenase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
38
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pH 7.6, half-life of free enzyme: 10 min, half-life of immobilized enzyme 5 h
40
43.3
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enzyme mFMO falls into the category of moderately stable enzymes with an apparent melting temperature of 43.3°C
45
46 - 50
differential scanning calorimetry (DSC) indicates that the thermal denaturation of the enzyme is irreversible in all cases. The melting temperature (Tm) for the wild-type enzyme and its polymorphic variants is in a range from 46°C to 50°C at pH 7.4. Calculation for the activation energy of unfolding is performed using a mathematical model, secondary structures of wild-type and mutant enzymes during heat inactivation, overview
50
additional information
40
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in absence of NADPH, residue 360 is important for thermal stability, half-lives of wild-type and mutant isozymes FMO1 and FMO3, overview
40
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purified recombinant FMO1, FMO3, and FMO5, the isozymes display similar thermal sensitivity, with activity decreased to 76% to 83% after 1 min preincubation at 40°C, 61% to 71% after 2 min preincubation, and 41% to 55% after 5 min preincubation
45
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the benzydamine N-oxygenation activity of the enzyme is reduced by approximately 70% by preheating at 45°C for 5 min. Benzydamine N-oxygenation is suppressed by 30% and 50% after preincubation of liver microsomes at 37°C for 5 and 10 min, respectively
45
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the benzydamine N-oxygenation activity of the enzyme is reduced by approximately 70% by preheating at 45°C for 5 min. Benzydamine N-oxygenation is suppressed by 30% and 50% after preincubation of liver microsomes at 37°C for 5 and 10 min, respectively
50
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10 min, elimination of most Fmo1 and Fmo3 activity, while 94% of Fmo2 activity remains
additional information
loss of about 30% of activity after heat treatment of mutant enzyme N413K, activity is preservable by NADPH
additional information
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loss of about 30% of activity after heat treatment of mutant enzyme N413K, activity is preservable by NADPH
additional information
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the lung isozyme shows high thermal stability as the liver isozyme
