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Ligand fenthion Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C1 0 H1 5 O3 PS2
fenthion
PNVJTZOFSHSLTO-UHFFFAOYSA-N
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
fenthion + NADPH + O2 = fenthion sulfoxide + NADP+ + H2O
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Substrate in Enzyme-catalyzed Reactions (5 results)
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fenthion + NADPH + O2 = fenthion sulfoxide + NADP+
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fenthion + NADPH + O2 = fenthion sulfoxide + NADP+ + H2O
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fenthion + NADPH + H+ + O2 = fenthion-oxon + sulfur + NADP+ + H2O
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fenthion + NADPH + H+ + O2 = fenthion-sulfoxide + NADP+ + H2O
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fenthion + [reduced NADPH-hemoprotein reductase] + O2 = ?
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Product in Enzyme-catalyzed Reactions (1 result)
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MPP precursor + H2O = MPP
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Activator in Enzyme-catalyzed Reactions (1 result)
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Inhibitor in Enzyme-catalyzed Reactions (1 result)
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Enzyme Kinetic Parameters
KM Value (27 results)
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0.145
-
wild-type enzyme, FMO3
0.15
-
mutant enzyme D132H, FMO3
0.2
-
mutant enzyme K158L, FMO3
0.22
-
mutant enzyme K158L/D132H, FMO3
0.24
-
mutant enzyme I303T, FMO1
0.3
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mutant enzyme R502X, FMO1
0.32
-
mutant enzyme H97Q, FMO1
0.34
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wild-type enzyme, FMO1
0.351
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mutant enzyme I303V, FMO1
0.0016
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desulfuration by recombinant human CYPs to fenthion-oxon
0.0022
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sulfoxidation to fenthion-sulfoxide
0.0024
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CYP2C19, at pH 7.4 and 37°C
0.0024
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CYP2C19, desulfuration by recombinant human CYPs to fenthion-oxon
0.0027
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desulfuration by recombinant human CYPs to fenthion-oxon
0.0044
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CYP2C19, at pH 7.4 and 37°C
0.0044
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CYP2C19, sulfoxidation to fenthion-sulfoxide
0.006
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CYP2C9, at pH 7.4 and 37°C
0.006
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CYP2C9, sulfoxidation to fenthion-sulfoxide
0.008
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CYP1A1, at pH 7.4 and 37°C
0.008
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CYP1A1, sulfoxidation to fenthion-sulfoxide
0.01
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sulfoxidation to fenthion-sulfoxide
0.012
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CYP2C9, at pH 7.4 and 37°C
0.012
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CYP2C9, desulfuration by recombinant human CYPs to fenthion-oxon
0.089
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CYP3A4, at pH 7.4 and 37°C
0.089
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CYP3A4, desulfuration by recombinant human CYPs to fenthion-oxon
0.131
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CYP3A4, at pH 7.4 and 37°C
0.131
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CYP3A4, sulfoxidation to fenthion-sulfoxide
Ki Value (2 results)
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0.0143
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pH 7.5, 25°C, recombinant enzyme
0.0221
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pH 7.5, 25°C, recombinant enzyme
IC50 Value (2 results)
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0.0807
-
pH 7.5, 25°C, recombinant enzyme
0.114
-
pH 7.5, 25°C, recombinant enzyme
References & Links Literature References (8)
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Matrix processing peptidase of mitochondria. Structure-function relationships
1990
Schneider, H.; Arretz, M.; Wachter, E.; Neupert, W.
J. Biol. Chem.
265
9881-9887
Efficient but aberrant cleavage of mitochondrial precursor proteins by the chloroplast stromal processing peptidase
1994
Bassham, D.C.; Creighton, A.M.; Arretz, M.; Brunner, M.; Robinson, C.
Eur. J. Biochem.
221
523-528
Evaluation of xenobiotic N- and S-oxidation by variant flavin-containing monooxygenase 1 (FMO1) enzymes
2004
Furnes, B.; Schlenk, D.
Toxicol. Sci.
78
196-203
Extrahepatic metabolism of carbamate and organophosphate thioether compounds by the flavin-containing monooxygenase and cytochrome P450 systems
2005
Furnes, B.; Schlenk, D.
Drug Metab. Dispos.
33
214-218
Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism
2005
Krueger, S.K.; Williams, D.E.
Pharmacol. Ther.
106
357-387
Synthesis of fenthion sulfoxide and fenoxon sulfoxide enantiomers: effect of sulfur chirality on acetylcholinesterase activity
2007
Gadepalli, R.S.; Rimoldi, J.M.; Fronczek, F.R.; Nillos, M.; Gan, J.; Deng, X.; Rodriguez-Fuentes, G.; Schlenk, D.
Chem. Res. Toxicol.
20
257-262
The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion
2008
Leoni, C.; Buratti, F.M.; Testai, E.
Toxicol. Appl. Pharmacol.
233
343-352
beta-Glucuronidase activity is a sensitive biomarker to assess low-level organophosphorus insecticide exposure
2010
Ueyama, J.; Satoh, T.; Kondo, T.; Takagi, K.; Shibata, E.; Goto, M.; Kimata, A.; Saito, I.; Hasegawa, T.; Wakusawa, S.; Kamijima, M.
Toxicol. Lett.
193
115-119
Links to other databases for fenthion
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