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(+)-camphor + [reduced NADPH-hemoprotein reductase] + O2
(+)-exo-5-hydroxycamphor + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
myrtenol + [oxidized NADPH-hemoprotein reductase] + H2O
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
pinene oxide + [oxidized NADPH-hemoprotein reductase] + H2O
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
verbenol + [oxidized NADPH-hemoprotein reductase] + H2O
(-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2
myrtanal + [oxidized NADPH-hemoprotein reductase] + H2O
(-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2
pino-carveol + [oxidized NADPH-hemoprotein reductase] + H2O
(1R)-cis-permethrin + O2 + [reduced NADPH-hemoprotein reductase]
3-phenoxybenzyl alcohol + 3-(4'-hydroxyphenoxy)-benzyl alcohol + [oxidized NADPH-hemoprotein reductase]
-
-
-
-
?
(1R)-trans-permethrin + O2 + [reduced NADPH-hemoprotein reductase]
3-phenoxybenzyl alcohol + 3-(4'-hydroxyphenoxy)-benzyl alcohol + [oxidized NADPH-hemoprotein reductase]
-
-
-
-
?
(1S)-cis-permethrin + O2 + [reduced NADPH-hemoprotein reductase]
3-phenoxybenzyl alcohol + 3-(4'-hydroxyphenoxy)-benzyl alcohol + [oxidized NADPH-hemoprotein reductase]
-
-
-
-
?
(1S)-trans-permethrin + O2 + [reduced NADPH-hemoprotein reductase]
3-phenoxybenzyl alcohol + 3-(4'-hydroxyphenoxy)-benzyl alcohol + [oxidized NADPH-hemoprotein reductase]
-
-
-
-
?
(methylsulfanyl)benzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
methyl(phenyl)sulfaniumolate + [oxidized NADPH-hemoprotein reductase] + ?
(R)-(+)-limonene + 2 O2 + 2 NADPH
(R)-cis-1,2-limonene epoxide + cis-carveol + 2 NADP+ + 2 H2O
(S)-(-)-limonene + NADPH + O2
(S)-trans-1,2 limonene epoxide + NADP+ + H2O
(S)-nicotine + [reduced NADPH-hemoprotein reductase] + O2
?
-
substrate of CYP3A4, the reaction involves electron transfer via FMN
-
-
?
1,4-dimethoxybenzene + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
1-chloro-4-(methylsulfanyl)benzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(4-chlorophenyl)(methyl)sulfaniumolate + [oxidized NADPH-hemoprotein reductase] + ?
1-chloro-4-ethenylbenzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(4-chlorophenyl)acetaldehyde + 2-(4-chlorophenyl)oxirane + 2-(4-chlorophenyl)ethan-1-ol + [oxidized NADPH-hemoprotein reductase] + ?
1-indanone + [reduced NADPH-hemoprotein reductase] + O2
(S)-3-hydroxy-1-indanone + [oxidized NADPH-hemoprotein reductase] + H2O
1-methoxy-4-(methylsulfanyl)benzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(4-methoxyphenyl)(methyl)sulfaniumolate + [oxidized NADPH-hemoprotein reductase] + ?
1-tetralone + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-1-tetralone + [oxidized NADPH-hemoprotein reductase] + H2O
10-p-nitrophenoxydecanoic acid + NADPH + O2
?
11-oxoprogesterone + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
12-methyl-myristic acid + NADPH + O2
?
-
CYP102A7
-
-
?
12-methyl-tetradecanoic acid + NADPH + O2
?
-
CYP102A7
-
-
?
13-methyl-myristic acid + NADPH + O2
?
-
CYP102A7
-
-
?
13-methyl-tetradecanoic acid + NADPH + O2
?
-
CYP102A7
-
-
?
2 3,5,4'-trimethoxy-trans-stilbene + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
3-hydroxy-5,4'-dimethoxy-trans-stilbene + 3,5-dihydroxy-4'-methoxy-trans-stilbene + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
2,3-dihydroindene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(1S)-2,3-dihydroinden-1-ol + 2,3-dihydroinden-1-one + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP1A2 catalyzes the first step of activation of the xenobiotic compound and its genotoxic effect, the second step is catalyzed by the sulfotransferase 1A1-1
-
-
?
2-amino-3-methylimidazo[4,5-f]quinoline + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP1A2 catalyzes the first step of activation of the xenobiotic compound and its genotoxic effect, the second step is catalyzed by the N(O)-acetyltransferase.
-
-
?
2-hydroxy-1-(4-hydroxyphenyl)guanidine + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
3 geranylacetone + 3 NADPH + 3 H+ + 3 O2
9,10-epoxygeranylacetone + 11-hydroxygeranylacetone + 5,6-epoxygeranylacetone + 3 NADP+ + 3 H2O
-
CYP102A7, high activity
-
-
?
3,5-dimethoxy-trans-stilbene + [reduced NADPH-hemoprotein reductase] + O2
?
3,7-dimethyl-1-octanol + [reduced NADPH-hemoprotein reductase] + O2
6-hydroxy-3,7-dimethyl-1-octanol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
3-cyano-7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
3-methoxybenzoic acid + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
when reconstituted with cytochrome P450 reductase 2, CYP53A15 converts 3-methoxybenzoic acid to 3,4-dihydroxybenzoic acid
-
-
?
3-methoxybenzoic acid + [reduced NADPH-hemoprotein reductase] + O2
3-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
when reconstituted with cytochrome P450 reductase 1, CYP53A15 converts 3-methoxybenzoic acid to 3-hydroxybenzoic acid
-
-
?
3-[2-(N,N-diethyl-N-methylammonium)ethyl]-7-methoxy-4-methylcoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
4-(methylnitrosamino)-1-(3pyridyl)-1-butanone + [reduced NADPH-hemoprotein reductase] + O2
?
4-androstene-3,17-dione + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
4-chlorothioanisole + [reduced NADPH-hemoprotein reductase] + H+ + O2
4-chlorothioanisole sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
Roseibium aggregatum
-
-
-
?
4-chlorothioanisole + [reduced NADPH-hemoprotein reductase] + O2
4-chlorothioanisole sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
4-fluorothioanisole + [reduced NADPH-hemoprotein reductase] + O2
4-fluorothioanisole sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
4-methoxythioanisole + [reduced NADPH-hemoprotein reductase] + O2
4-methoxythioanisole sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
4-nitroanisole + [reduced NADPH-hemoprotein reductase] + H+ + O2
4-nitrophenol + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
4-tert-butylcyclohexyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
4-tolylmethylsulfide + [reduced NADPH-hemoprotein reductase] + O2
4-tolylmethylsulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
6-methoxy-1-tetralone + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-6-methoxy-1-tetralone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
6beta-hydroxytestosterone + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
7-ethoxy-4-trifluoromethylcoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxy-4-trifluoromethylcoumarin + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP1A2 cooperates with NADPH-cytochrome P450 reductase, which provides NADPH for the reaction. Interaction with their redox partner, NADPH-cytochrome P450 reductase, i.e. CPR, in a 1:1 molar ratio
-
-
?
7-ethoxy-trifluoromethylcoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
O-deethylation
-
-
?
7-ethoxycoumarin + NADPH + H+ + O2
7-hydroxycoumarin + NADP+ + H2O + ?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + H+
coumarin + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
7-ethoxyresorufin + O2 + reduced donor
?
-
7-ethoxyresorufin O-deethylation
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
resorufin + ethanol + [oxidized NADPH-hemoprotein reductase] + H2O
7-hydroxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
7-methoxy-1-tetralone + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-7-methoxy-1-tetralone + [oxidized NADPH-hemoprotein reductase] + H2O
7-methoxy-4-(trifluoromethyl)-coumarin + [reduced NADPH-hemoprotein reductase] + O2
?
7-methoxycoumarin + [reduced NADPH-hemoprotein reductase] + H+
coumarin + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
7-methoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + ?
-
-
-
-
?
7-methoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
7-methoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
7-propoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
acenaphthene + [reduced NADPH-hemoprotein reductase] + O2
1-acenaphthenol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
adrenic acid + [reduced NADPH-hemoprotein reductase] + O2
?
aflatoxin B1 + [reduced NADPH-hemoprotein reductase] + O2
?
alpha-ionone + NADPH + O2
?
-
CYP102A7, high activity
-
-
?
alpha-ionone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
alpha-santonin + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
ambroxide + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
aminopyrine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
amiprofos-methyl + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
androsterone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
anisole + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
anthraquinone-1,5-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
anthraquinone-1,8-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
anthraquinone-1-sulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
anthraquinone-2,6-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
anthraquinone-2-sulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
3',8-dihydroxyapigenin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + 11,12-epoxyeicosa-5,8,14-trienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyeicosatetraenoic acid + 19-hydroxyeicosatetraenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
ratio 12:1
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
aryl hydrocarbons + [reduced NADPH-hemoprotein reductase] + O2
?
avermectin + [reduced NADPH-hemoprotein reductase] + O2
4''-oxo-avermectin + [oxidized NADPH-hemoprotein reductase] + H2O
bentazon + [reduced NADPH-hemoprotein reductase] + O2
?
-
ring-hydroxylation
-
-
?
benzo(a)pyrene + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
benzo(ghi)perylene + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
benzo-pyrene + [reduced NADPH-hemoprotein reductase] + O2
?
-
recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
when reconstituted with cytochrome P450 reductase 2, CYP53A15 converts benzoic acid to 3,4-dihydroxybenzoic acid
-
-
?
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
when reconstituted with cytochrome P450 reductase 1, CYP53A15 converts benzoic acid to 4-hydroxybenzoic acid
-
-
?
benzyl methyl sulfide + [reduced NADPH-hemoprotein reductase] + O2
benzyl methyl sulfoxide + benzyl methyl sulfone + [oxidized NADPH-hemoprotein reductase] + H2O
-
50% conversion
product ratio of 78:22
-
?
bergapten + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
beta-damasone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
beta-ionol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
beta-ionone + NADPH + O2
4-hydroxy-beta-ionone + NADP+ + H2O
-
CYP102A7, high activity
-
-
?
beta-ionone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
beta-ionone + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxy-beta-ionone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
beta-ionone + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
substrate only for mutant A74G/F88V/S189Q
-
-
?
bispyribac-sodium + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
bornyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
capric acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
capric acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
about 10% of the activity with palmitic acid, wild-type
-
-
?
caprylic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
substrate only for mutant A74G/F88V/S189Q
-
-
?
chlormadinone acetate + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
chlorzoxazone + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
cinnamic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
cis-nerolidol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
compactin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
coumarin + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cytochrome c + NADH + H+ + O2
?
cytochrome c + O2 + NADH
?
cytochrome c + O2 + NADH
? + NAD+ + ?
Roseibium aggregatum
-
-
-
?
daidzein + [reduced NADPH-hemoprotein reductase] + O2
3'-hydroxydaidzein + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
decanoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
dehydroepiandrosterone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
dibenzylfluorescein + [reduced NADPH-hemoprotein reductase] + O2
?
diclofop + [reduced NADPH-hemoprotein reductase] + O2
?
-
ring-hydroxylation
-
-
?
dimethylaniline + [reduced NADPH-hemoprotein reductase] + O2
?
-
substrate of CYP3A4
-
-
?
docosahexaenoic acid + [reduced NADPH-hemoprotein reductase] + O2
22-hydroxydocosahexaenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
dodecanoic acid + NADPH + O2
?
-
CYP102A7
-
-
?
dodecanoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
isozyme CYP52A17, good substrate
-
-
?
eicosapentaenoic acid + NADPH + H+ + O2
20-hydroxyeicosapentaenoic acid + NADP+ + H2O
-
-
-
-
?
eicosapentaenoic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyeicosapentaenoic acid + 19-hydroxyeicosapentaenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
ratio 4:3
-
?
eicosapentaenoic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyeicosapentaenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
eicosenoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
elymoclavine + [reduced NADPH-hemoprotein reductase] + O2
paspalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
eriodictyol + [reduced NADPH-hemoprotein reductase] + O2
6-hydroxyeriodictyol + 8-hydroxyeriodictyol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
erythromycin + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
estrone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
ethyl methyl sulfide + [reduced NADPH-hemoprotein reductase] + O2
ethyl methyl sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
ethyl phenyl sulfide + [reduced NADPH-hemoprotein reductase] + O2
ethyl phenyl sulfoxide + ethyl phenyl sulfone + [oxidized NADPH-hemoprotein reductase] + H2O
-
70% conversion
product ratio of 52:18
-
?
ethylbenzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(1S)-1-phenylethan-1-ol + 1-phenylethan-1-one + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
ethylbenzene + [reduced NADPH-hemoprotein reductase] + O2
(R)-1-phenylethanol + 1-phenylethanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
product ratio of 88:12
-
?
ethylbenzene + [reduced NADPH-hemoprotein reductase] + O2
1-phenylethyl alcohol + 2-phenylethyl alcohol + [reduced NADPH-hemoprotein reductase] + O2
recombinant enzyme
-
-
?
farnesol + [reduced NADPH-hemoprotein reductase] + O2
?
CYP102A1 oxidizes farnesol to three products (2,3-epoxyfarnesol, 10,11-epoxyfarnesol, and 9-hydroxyfarnesol), whereas CYP4C7 produces 12-hydroxyfarnesol as the major product. Chimeric proteins C(78-82,F87L) and C(78-82,F87L,328-330) show the most complete change in substrate selectivity from fatty acids to farnesol, and both retain superior enzyme activity with respect to CYP102A1 approximately 5times and approximately 2times greater, respectively. C(78-82,F87L,328-330) produces 12-hydroxyfarnesol as the major metabolite, as does CYP4C7
-
-
?
fenchyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
fenoxaprop-ethyl + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
fenthion + NADPH + H+ + O2
fenthion-oxon + sulfur + NADP+ + H2O
-
-
-
r
fenthion + NADPH + H+ + O2
fenthion-sulfoxide + NADP+ + H2O
-
-
-
r
fenthion + [reduced NADPH-hemoprotein reductase] + O2
?
fenthion-sulfoxide and fenthion-oxon, are formed by some CYPs although at very different levels, depending on the relative CYP hepatic content. Fenthion-oxon formation is favored and at low fenthion concentrations CYP2B6 and CYP1A2 are mainly involved in its formation. At higher levels, a more widespread CYP involvement is evident, as in the case of fenthion-sulfoxide
-
-
?
fenthion-sulfoxide + [reduced NADPH-hemoprotein reductase] + O2
fenthion-sulfone + [oxidized NADPH-hemoprotein reductase] + H2O
fluoranthene + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
fluorene + [reduced NADPH-hemoprotein reductase] + O2
9-fluorenol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
fluoxetine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
genistein + [reduced NADPH-hemoprotein reductase] + O2
3',8-dihydroxygenistein + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
geraniol + [reduced NADPH-hemoprotein reductase] + O2
8-hydroxygeraniol + 10-hydroxygeraniol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
giberellic acid GA12 + [reduced NADPH-hemoprotein reductase] + O2
16alpha,17-epoxy GA12 + [oxidized NADPH-hemoprotein reductase] + H2O
-
product identification by GC-MS, the epoxid is transformed into 16,17-dihydro-16alpha,17-dihydroxy-GA4 under acidic conditions with acidic acid
-
?
giberellic acid GA4 + [reduced NADPH-hemoprotein reductase] + O2
16alpha,17-epoxy GA4 + [oxidized NADPH-hemoprotein reductase] + H2O
giberellic acid GA9 + [reduced NADPH-hemoprotein reductase] + O2
16alpha,17-epoxy GA9 + [oxidized NADPH-hemoprotein reductase] + H2O
-
product identification by GC-MS, the epoxid is transformed into 16,17-dihydro-16alpha,17-dihydroxy-GA4 under acidic conditions with acidic acid
-
?
hexadecanoic acid + NADPH + O2
?
-
CYP102A7, highest binding affinity
-
-
?
indane + [reduced NADPH-hemoprotein reductase] + O2
(S)-3-hydroxy-indane + [oxidized NADPH-hemoprotein reductase] + H2O
indene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(S)-inden-1-ol + 2,3-dihydroinden-1-one + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
indene + [reduced NADPH-hemoprotein reductase] + O2
indenol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
indole + [reduced NADPH-hemoprotein reductase] + O2
(2Z)-2-(3-oxo-1,3-dihydro-2H-indol-2-ylidene)-1,2-dihydro-3H-indol-3-one + (3Z)-3-(3-oxo-1,3-dihydro-2H-indol-2-ylidene)-1,3-dihydro-2H-indol-2-one + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
isopimpinellin + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
ketoconazole + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
lauric acid + NADPH + O2
?
-
CYP102A7
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
linoleic acid + NADPH + O2
?
-
CYP102A1, CYP102A2, CYP102A3 and CYP102A7. CYP102A7 with high binding affinity
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
(9Z,12Z)-18-hydroxyoctadeca-9,12-dienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
isozyme CYP52A17, good substrate, isozyme CYP52A13, good substrate
-
-
?
losartan + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
luteolin + [reduced NADPH-hemoprotein reductase] + O2
3',8-dihydroxyapigenin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
m-xylene + [reduced NADPH-hemoprotein reductase] + O2
3-methylbenzyl alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
recombinant enzyme
-
-
?
macrolide YC-17 + [reduced NADPH-hemoprotein reductase] + O2
methymycin + [oxidized NADPH-hemoprotein reductase] + H2O
-
Hydroxylation of C-10 position yield methymycin and of the C-12 neomethymycin. Hydroxylation at both positions yields novamethymycin.
-
-
?
macrolide YC-17 + [reduced NADPH-hemoprotein reductase] + O2
neomethymycin + [oxidized NADPH-hemoprotein reductase] + H2O
-
Hydroxylation of C-10 position yield methymycin and of the C-12 neomethymycin. Hydroxylation at both positions yields novamethymycin.
-
-
?
macrolide YC-17 + [reduced NADPH-hemoprotein reductase] + O2
novamethymycin + [oxidized NADPH-hemoprotein reductase] + H2O
-
Hydroxylation of C-10 position yield methymycin and of the C-12 neomethymycin. Hydroxylation at both positions yields novamethymycin.
-
-
?
medroxyprogesterone acetate + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
mefenacet + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
methyl 10,11-epoxyfarnesoate + [reduced NADPH-hemoprotein reductase] + O2
?
the major product of C(78-82,F87L,328-330) during 10,11-epoxymethylfarnesoate oxidation is determined to be the 12-hydroxy isomer
-
-
?
methyl 4-methylphenyl sulfide + [reduced NADPH-hemoprotein reductase] + O2
methyl 4-methylphenyl sulfoxide + methyl 4-methylphenyl sulfone + [oxidized NADPH-hemoprotein reductase] + H2O
-
41% conversion
product ratio of 95:5
-
?
methyl farnesoate + O2 + NADPH
?
the major product of C(78-82,F87L,328-330) during methylfarnesoate oxidation is determined to be the 12-hydroxy isomer
-
-
?
methyl phenyl sulfide + O2 + NADH
methyl phenyl sulfoxide + methyl phenyl sulfone + NAD+ + H2O
-
55% conversion
product ratio of 77:23
-
?
methyltestosterone + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
metolachlor + [reduced NADPH-hemoprotein reductase] + O2
?
Sorghum sp.
-
de-ethylation
-
-
?
midazolam + [reduced NADPH-hemoprotein reductase] + O2
1'-hydroxymidazolam + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
myristic acid + NADPH + O2
?
-
CYP102A7
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
omega-hydroxy-myristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
isozyme CYP52A17, best substrate
isoform CYP52A17, additional fornmation of about 15% dicarbonic acid
-
?
N'-nitrosonornicotine + [reduced NADPH-hemoprotein reductase] + O2
?
N-acetylindole + [reduced NADPH-hemoprotein reductase] + O2
1-acetyl-1,2-dihydro-3H-indol-3-one + 1-acetyl-1,3-dihydro-2H-indol-2-one + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
naphthalene + [reduced NADPH-hemoprotein reductase] + O2
1-naphthol + H2O + [oxidized NADPH-hemoprotein reductase] + H2O
regioselective oxidation
-
-
?
naphthalene + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
substrate only for mutant A74G/F88V/S189Q
-
-
?
narbomycin + [reduced NADPH-hemoprotein reductase] + O2
pikromycin + [oxidized NADPH-hemoprotein reductase] + H2O
naringenin + [reduced NADPH-hemoprotein reductase] + O2
eriodictyol + 6-hydroxyeriodictyol + 8-hydroxyeriodictyol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
neryl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
nerylacetone + NADPH + O2
9,10-epoxynerylacetone + 5,6-epoxynerylacetone + NADP+ + H2O
-
CYP102A7, high activity
-
-
?
nonylphenol + [reduced NADPH-hemoprotein reductase] + O2
?
nootkatone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
norflurazon + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
octane + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
substrate only for mutant A74G/F88V/S189Q and for mutant A74G/S189Q
-
-
?
okadaic acid + NADPH + O2
?
okadaic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
oleandomycin + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxy-oleandomycin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
oleic acid + NADPH + O2
?
-
CYP102A1, CYP102A2, CYP102A3 and CYP102A7
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
omega-hydroxy oleic acid + n-decan-dicarboxylic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
isozyme CYP52A13, best substrate,isozyme CYP52A17, good substrate
isozyme CYP52A13, products in ratio 1:1, CYP52A17, ratio 3:7 of hydroxy- and dicarboxy-product
-
?
omega-(p-nitrophenyl)decanoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
omega-(p-nitrophenyl)dodecanoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
omega-(p-nitrophenyl)octanoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
p-chlorothioanisole + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
p-fluorothioanisole + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
p-methoxythioanisole + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
p-nitrophenol + [reduced NADPH-hemoprotein reductase] + O2
?
p-tolyl methyl sulfide + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
p-xylene + O2 + [reduced NADPH-hemoprotein reductase]
2,5-dimethylphenol + H2O + [oxidized NADPH-hemoprotein reductase]
paclitaxel + [reduced NADPH-hemoprotein reductase] + O2
6alpha-hydroxypaclitaxel + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitic acid + NADPH + O2
?
-
CYP102A7
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
palmitoleic acid + NADPH + O2
?
-
CYP102A7
-
-
?
pendimethalin + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
phenanthrene + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
phenyl ethyl sulfide + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
phenyl methyl sulfide + [reduced NADPH-hemoprotein reductase] + O2
phenyl methyl sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
pilocarpine + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
pregnenolone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
progesterone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
progesterone + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
propylbenzene + [reduced NADPH-hemoprotein reductase] + O2
(R)-1-phenyl-1-propanol + (R)-1-phenyl-1-propanol + 1-phenylpropan-1-one + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
product ratio of 79:7:14
-
?
prostaglandin + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin + [oxidized NADPH-hemoprotein reductase] + H2O
-
physiological functions are the metabolic inactivation of prostaglandins and the production of 20-hydroxyeicosatetraenoic acid, CYP4A4
-
-
?
prostaglandin A1 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin A1 + [oxidized NADPH-hemoprotein reductase] + H2O
prostaglandin A2 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin A2 + [oxidized NADPH-hemoprotein reductase] + H2O
prostaglandin D2 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin D2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4A4
-
-
?
prostaglandin E1 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin E1 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4A4
-
-
?
prostaglandin E2 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin E2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4A4
-
-
?
prostaglandin F2alpha + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin F2alpha + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4A4
-
-
?
psoralen + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
pyrene + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
pyributicarb + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
quinine + [reduced NADPH-hemoprotein reductase] + O2
3-hydroxyquinine + [oxidized NADPH-hemoprotein reductase] + H2O
RH + [reduced NADPH-hemoprotein reductase] + O2
ROH + [oxidized NADPH-hemoprotein reductase] + H2O
rivaroxaban + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
S-mephenytoin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
sclareolide + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
sertraline + [reduced NADPH-hemoprotein reductase] + O2
demethylsertraline + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
simvastatin + [reduced NADPH-hemoprotein reductase] + O2
6-beta-hydroxy-methyl-simvastatin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
stanolone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
stearic acid + NADPH + O2
?
-
CYP102A7
-
-
?
stearic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
stearic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
styrene + O2 + H2O2
(R)-styrene oxide + (S)-styrene oxide + H2O
-
engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH
-
-
?
styrene + O2 + NAD(P)H
(R)-styrene oxide + (S)-styrene oxide + H2O + NAD(P)+
-
-
enantioselective styrene oxidation with different CYP102A1 mutants, 25% S-isomer for the wild-type enzyme, 58% S-isomer for mutant A74E/F87V/P386S, 49% R-isomer for mutant F87A, 65% R-isomer for mutant A74G/F87V/L188Q, and 92% R-isomer for mutant F87G
-
?
styrene + O2 + reduced putidaredoxin
(S)-styrene oxide + 2-phenylethanol + oxidized putidaredoxin + H2O
-
-
product ratio of 81:19
-
?
testosterone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
testosterone + [reduced NADPH-hemoprotein reductase] + O2
6beta-hydroxytestosterone + [oxidized NADPH-hemoprotein reductase] + H2O
testosterone + [reduced NADPH-hemoprotein reductase] + O2
?
testosterone enanthate + [reduced NADPH-hemoprotein reductase] + O2
?
CYP107
-
-
?
tetradecanoic acid + NADPH + O2
?
-
CYP102A7, highest activity
-
-
?
tetralin + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
tetralin + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-tetralin + [oxidized NADPH-hemoprotein reductase] + H2O
thiobencarb + O2 + reduced flavoprotein
?
-
-
-
-
?
tolbutamide + [reduced NADPH-hemoprotein reductase] + O2
?
toluene + O2 + NAD(P)H + cytochrome c
benzyl alcohol + H2O + NAD(P)+ + reduced cytochrome c
-
-
-
?
toluene + O2 + NADH
?
-
-
-
-
?
toluene + [reduced NADPH-hemoprotein reductase] + H+ + O2
benzylalcohol + benzaldehyde + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
trans-decahydronaphthalene + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
trifluralin + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
-
-
-
-
?
vandetanib + [reduced NADPH-hemoprotein reductase] + H+ + O2
N-desmethylvandetanib + [oxidized NADPH-hemoprotein reductase] + ?
-
-
-
?
xanthotoxin + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
additional information
?
-
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
myrtenol + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/F87G/L188Q
mutant A74G/F87G/L188Q, 13% pinene oxide, 77% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
myrtenol + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/F87V/L188Q
mutant A74G/F87V/L188Q, 70% pinene oxide, 20% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
pinene oxide + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/F87G/L188Q
mutant A74G/F87V/L188Q, 13% pinene oxide, 77% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
pinene oxide + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/F87V/L188Q
mutant A74G/F87V/L188Q, 70% pinene oxide, 20% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
pinene oxide + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/L188Q
mutant A74G/L188Q, 85% pinene oxide, 15% verbenol
-
?
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
verbenol + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/F87G/L188Q
mutant A74G/F87G/L188Q, 13% pinene oxide, 77% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
verbenol + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/F87V/L188Q
mutant A74G/F87V/L188Q, 70% pinene oxide, 20% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2
verbenol + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/L188Q
mutant A74G/L188Q, 85% pinene oxide, 15% verbenol
-
?
(-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2
myrtanal + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/F87G/L188Q
mutant A74G/F87G/L188Q, 40% pino-carveol, 60% myrtanal
-
?
(-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2
myrtanal + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/F87V/L188Q
mutant A74G/F87V/L188Q, 68% pino-carveol, 32% myrtanal
-
?
(-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2
pino-carveol + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/F87G/L188Q
mutant A74G/F87G/L188Q, 40% pino-carveol, 60% myrtanal
-
?
(-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2
pino-carveol + [oxidized NADPH-hemoprotein reductase] + H2O
mutant A74G/F87V/L188Q
mutant A74G/F87V/L188Q, 68% pino-carveol, 32% myrtanal
-
?
(methylsulfanyl)benzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
methyl(phenyl)sulfaniumolate + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
(methylsulfanyl)benzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
methyl(phenyl)sulfaniumolate + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum DSM 13394
-
-
-
?
(R)-(+)-limonene + 2 O2 + 2 NADPH
(R)-cis-1,2-limonene epoxide + cis-carveol + 2 NADP+ + 2 H2O
-
CYP102A7, high activity
-
-
?
(R)-(+)-limonene + 2 O2 + 2 NADPH
(R)-cis-1,2-limonene epoxide + cis-carveol + 2 NADP+ + 2 H2O
-
CYP102A7, high activity
-
-
?
(S)-(-)-limonene + NADPH + O2
(S)-trans-1,2 limonene epoxide + NADP+ + H2O
-
CYP102A7, high activity
-
-
?
(S)-(-)-limonene + NADPH + O2
(S)-trans-1,2 limonene epoxide + NADP+ + H2O
-
CYP102A7, high activity
-
-
?
1-chloro-4-(methylsulfanyl)benzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(4-chlorophenyl)(methyl)sulfaniumolate + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
1-chloro-4-(methylsulfanyl)benzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(4-chlorophenyl)(methyl)sulfaniumolate + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum DSM 13394
-
-
-
?
1-chloro-4-ethenylbenzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(4-chlorophenyl)acetaldehyde + 2-(4-chlorophenyl)oxirane + 2-(4-chlorophenyl)ethan-1-ol + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
1-chloro-4-ethenylbenzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(4-chlorophenyl)acetaldehyde + 2-(4-chlorophenyl)oxirane + 2-(4-chlorophenyl)ethan-1-ol + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum DSM 13394
-
-
-
?
1-indanone + [reduced NADPH-hemoprotein reductase] + O2
(S)-3-hydroxy-1-indanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
1-indanone + [reduced NADPH-hemoprotein reductase] + O2
(S)-3-hydroxy-1-indanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
1-methoxy-4-(methylsulfanyl)benzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(4-methoxyphenyl)(methyl)sulfaniumolate + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum
-
-
-
?
1-methoxy-4-(methylsulfanyl)benzene + [reduced NADPH-hemoprotein reductase] + H+ + O2
(4-methoxyphenyl)(methyl)sulfaniumolate + [oxidized NADPH-hemoprotein reductase] + ?
Roseibium aggregatum DSM 13394
-
-
-
?
1-tetralone + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-1-tetralone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
1-tetralone + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-1-tetralone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
10-p-nitrophenoxydecanoic acid + NADPH + O2
?
-
CYP102A7
-
-
?
10-p-nitrophenoxydecanoic acid + NADPH + O2
?
-
CYP102A7
-
-
?
2 3,5,4'-trimethoxy-trans-stilbene + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
3-hydroxy-5,4'-dimethoxy-trans-stilbene + 3,5-dihydroxy-4'-methoxy-trans-stilbene + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
2 3,5,4'-trimethoxy-trans-stilbene + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
3-hydroxy-5,4'-dimethoxy-trans-stilbene + 3,5-dihydroxy-4'-methoxy-trans-stilbene + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
3,5-dimethoxy-trans-stilbene + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
3,5-dimethoxy-trans-stilbene + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
3-cyano-7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
3-cyano-7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
CYP2C19
-
-
?
4-(methylnitrosamino)-1-(3pyridyl)-1-butanone + [reduced NADPH-hemoprotein reductase] + O2
?
-
nicotine oxidase activity of CYP2A6, activates the tobacco-derived carcinogens to mutagenic products
-
-
?
4-(methylnitrosamino)-1-(3pyridyl)-1-butanone + [reduced NADPH-hemoprotein reductase] + O2
?
-
nicotine oxidase activity of CYP2A6
-
-
?
4-androstene-3,17-dione + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
4-androstene-3,17-dione + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
4-tert-butylcyclohexyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
4-tert-butylcyclohexyl acetate + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
7-ethoxycoumarin + NADPH + H+ + O2
7-hydroxycoumarin + NADP+ + H2O + ?
-
CYP102A7 catalyses dealkylation, although with activity much lower than towards fatty acids
-
-
?
7-ethoxycoumarin + NADPH + H+ + O2
7-hydroxycoumarin + NADP+ + H2O + ?
-
mediates the O-dealkylation
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
-
wild-type enzyme and recombinant enzyme P4502B6 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
-
wild-type enzyme and recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
-
-
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
O-dealkylation
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxycoumarin O-deethylation
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxycoumarin O-deethylation
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxycoumarin O-deethylation
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxyresorufin O-deethylation
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxyresorufin O-deethylation
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxyresorufin O-deethylation
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
resorufin + ethanol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
resorufin + ethanol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
7-methoxy-1-tetralone + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-7-methoxy-1-tetralone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
7-methoxy-1-tetralone + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-7-methoxy-1-tetralone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
7-methoxy-4-(trifluoromethyl)-coumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
7-methoxy-4-(trifluoromethyl)-coumarin + [reduced NADPH-hemoprotein reductase] + O2
?
CYP2C9, CYP2E1
-
-
?
adrenic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
i.e. all-cis-7,10,13,16-docosatetraenoic acid
-
-
?
adrenic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
i.e. all-cis-7,10,13,16-docosatetraenoic acid
-
-
?
adrenic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
i.e. all-cis-7,10,13,16-docosatetraenoic acid
-
-
?
aflatoxin B1 + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
aflatoxin B1 + [reduced NADPH-hemoprotein reductase] + O2
?
-
i.e. AFB1, bioactivation of the carcinogenic mycotoxin to a toxic compound, although not acutely toxic at low concentrations, AFB1 had significant chronic effects, including protracted development, increased mortality, decreased pupation rate, and reduced pupal weight, sensitivity varies with developmental stage, whereas intermediate concentrations causes complete mortality in first instars, this same concentration has no detectable adverse effects on larvae encountering AFB1 in fifth instar. These compounds owe their toxicity to their ability to form irreversible adducts to nucleic acids with the concomitant inhibition of DNA replication and DNA-dependent transcription, mortality, overview
-
-
?
alpha-ionone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-ionone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-santonin + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-santonin + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
ambroxide + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
ambroxide + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
aminopyrine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
aminopyrene-N-demethylation
-
-
?
aminopyrine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
aminopyrine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
aminopyrene-N-demethylation
-
-
?
aminopyrine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
aminopyrene-N-demethylation
-
-
?
androsterone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
androsterone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
anthraquinone-1,5-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity only in roots
-
-
?
anthraquinone-1,5-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity only in roots
-
-
?
anthraquinone-1,5-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity only in shoots
-
-
?
anthraquinone-1,8-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity only in roots
-
-
?
anthraquinone-1,8-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity only in shoots
-
-
?
anthraquinone-1-sulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity in shoots and roots
-
-
?
anthraquinone-1-sulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity in shoots and roots
-
-
?
anthraquinone-1-sulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity only in shoots
-
-
?
anthraquinone-2,6-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity in shoots and roots
-
-
?
anthraquinone-2,6-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity in shoots and roots
-
-
?
anthraquinone-2,6-disulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity in shoots and roots
-
-
?
anthraquinone-2-sulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity in shoots and roots
-
-
?
anthraquinone-2-sulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity in shoots and roots
-
-
?
anthraquinone-2-sulfonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
activity in shoots and roots
-
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
-
CYP102A7
-
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
-
CYP102A7
-
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
-
-
i.e. 20-HETE, a potent constrictor of renal microvessels and inhibits Na+ reabsorption in the proximal tubule and thick ascending limb, i.e.20-HETE
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
-
-
i.e. 20-HETE, a potent constrictor of renal microvessels and inhibits Na+ reabsorption in the proximal tubule and thick ascending limb, i.e.20-HETE
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + 11,12-epoxyeicosa-5,8,14-trienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
reaction products generated by isoform CYP102B1
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + 11,12-epoxyeicosa-5,8,14-trienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
reaction products generated by isoform CYP102B1
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
reaction products generated by isoform CYP102A1
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
reaction products generated by isoform CYP102A1
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
aryl hydrocarbons + [reduced NADPH-hemoprotein reductase] + O2
?
-
e.g. benzo[a]pyrene, ethoxyresuforin, biphenyl, p-nitroanisole, acetanilide, 2-acetylaminofluorene, 2-ethoxycoumarin, estradiol-17beta, testosterone
-
-
?
aryl hydrocarbons + [reduced NADPH-hemoprotein reductase] + O2
?
-
prostaglandins
-
-
?
avermectin + [reduced NADPH-hemoprotein reductase] + O2
4''-oxo-avermectin + [oxidized NADPH-hemoprotein reductase] + H2O
-
4''-oxo-avermectin is a key intermediate in the manufacture of the agriculturally important insecticide emamectin benzoate from the natural product avermectin, overview
-
-
?
avermectin + [reduced NADPH-hemoprotein reductase] + O2
4''-oxo-avermectin + [oxidized NADPH-hemoprotein reductase] + H2O
-
avermectin oxidation activity
-
-
?
avermectin + [reduced NADPH-hemoprotein reductase] + O2
4''-oxo-avermectin + [oxidized NADPH-hemoprotein reductase] + H2O
-
4''-oxo-avermectin is a key intermediate in the manufacture of the agriculturally important insecticide emamectin benzoate from the natural product avermectin, overview
-
-
?
avermectin + [reduced NADPH-hemoprotein reductase] + O2
4''-oxo-avermectin + [oxidized NADPH-hemoprotein reductase] + H2O
-
avermectin oxidation activity
-
-
?
bergapten + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
bergapten + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-damasone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-damasone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-ionol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-ionol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-ionone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-ionone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
recombinant wild-type enzyme and enzyme mutant fused to yeast reductase expressed in transgenic potato plants
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
ring methyl-hydroxylation
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group, recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
ring methyl-hydroxylation
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cis-nerolidol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cis-nerolidol + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cytochrome c + NADH + H+ + O2
?
-
-
-
-
r
cytochrome c + NADH + H+ + O2
?
-
-
-
-
r
cytochrome c + NADH + H+ + O2
?
-
-
-
r
cytochrome c + O2 + NADH
?
-
-
-
-
r
cytochrome c + O2 + NADH
?
-
-
-
-
r
cytochrome c + O2 + NADH
?
-
-
-
r
decanoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
decanoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dehydroepiandrosterone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dehydroepiandrosterone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dibenzylfluorescein + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
dibenzylfluorescein + [reduced NADPH-hemoprotein reductase] + O2
?
CYP3A4, CYP19
-
-
?
docosahexaenoic acid + [reduced NADPH-hemoprotein reductase] + O2
22-hydroxydocosahexaenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
docosahexaenoic acid + [reduced NADPH-hemoprotein reductase] + O2
22-hydroxydocosahexaenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
docosahexaenoic acid + [reduced NADPH-hemoprotein reductase] + O2
22-hydroxydocosahexaenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
elymoclavine + [reduced NADPH-hemoprotein reductase] + O2
paspalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
the product is the precursor for D-lysergic acid
-
?
elymoclavine + [reduced NADPH-hemoprotein reductase] + O2
paspalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
the product is the precursor for D-lysergic acid
-
?
estrone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
estrone + [reduced NADPH-hemoprotein reductase] + H+ + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
fenthion-sulfoxide + [reduced NADPH-hemoprotein reductase] + O2
fenthion-sulfone + [oxidized NADPH-hemoprotein reductase] + H2O
CYP1A1, CYP2C9 and CYP3A4 form only traces or negligible levels of fenthion-sulfone
-
-
?
fenthion-sulfoxide + [reduced NADPH-hemoprotein reductase] + O2
fenthion-sulfone + [oxidized NADPH-hemoprotein reductase] + H2O
CYP1A2 forms only traces or negligible levels of fenthion-sulfone
-
-
?
fenthion-sulfoxide + [reduced NADPH-hemoprotein reductase] + O2
fenthion-sulfone + [oxidized NADPH-hemoprotein reductase] + H2O
CYP2B6 forms only traces or negligible levels of fenthion-sulfone
-
-
?
giberellic acid GA4 + [reduced NADPH-hemoprotein reductase] + O2
16alpha,17-epoxy GA4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
the product is transformed further to 16,17-dihydro-16alpha,17-dihydroxy-GA4 in the plant, product identification by GC-MS, the epoxid is transformed into 16,17-dihydro-16alpha,17-dihydroxy-GA4 under acidic conditions with acidic acid
-
?
giberellic acid GA4 + [reduced NADPH-hemoprotein reductase] + O2
16alpha,17-epoxy GA4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
product identification by GC-MS, the epoxid is transformed into 16,17-dihydro-16alpha,17-dihydroxy-GA4 under acidic conditions with acidic acid
-
?
indane + [reduced NADPH-hemoprotein reductase] + O2
(S)-3-hydroxy-indane + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
indane + [reduced NADPH-hemoprotein reductase] + O2
(S)-3-hydroxy-indane + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
ketoconazole + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
-
-
-
?
ketoconazole + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
?
products of hydroxylation by wild-type CYP102A1 are 11-OH, 10-OH, 9-OH, 8-OH, 7-OH, and 6-OH, corresponding to omega-1 to omega-6 hydroxylation
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
(9Z,12Z)-18-hydroxyoctadeca-9,12-dienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
(9Z,12Z)-18-hydroxyoctadeca-9,12-dienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
(9Z,12Z)-18-hydroxyoctadeca-9,12-dienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
N'-nitrosonornicotine + [reduced NADPH-hemoprotein reductase] + O2
?
-
nicotine oxidase activity of CYP2A6, activates the tobacco-derived carcinogens to mutagenic products
-
-
?
N'-nitrosonornicotine + [reduced NADPH-hemoprotein reductase] + O2
?
-
nicotine oxidase activity of CYP2A6
-
-
?
narbomycin + [reduced NADPH-hemoprotein reductase] + O2
pikromycin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
narbomycin + [reduced NADPH-hemoprotein reductase] + O2
pikromycin + [oxidized NADPH-hemoprotein reductase] + H2O
-
the organism is a pikromycin producer
-
-
?
nonylphenol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
nonylphenol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
okadaic acid + NADPH + O2
?
-
-
-
-
?
okadaic acid + NADPH + O2
?
-
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
p-nitrophenol + [reduced NADPH-hemoprotein reductase] + O2
?
CYP2E1
-
-
?
p-nitrophenol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
p-xylene + O2 + [reduced NADPH-hemoprotein reductase]
2,5-dimethylphenol + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
p-xylene + O2 + [reduced NADPH-hemoprotein reductase]
2,5-dimethylphenol + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
?
products of hydroxylation by wild-type CYP102A1 are 15-OH, 14-OH, 13-OH, 12-OH, 11-OH, and 10-OH, corresponding to omega-1 to omega-6 hydroxylation, with omega-1 to omega-3 being the major products in both cases
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
isozyme CYP52A17, good substrate
-
-
?
prostaglandin A1 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin A1 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4A4
-
-
?
prostaglandin A1 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin A1 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4A6
-
-
?
prostaglandin A1 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin A1 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4A7
-
-
?
prostaglandin A2 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin A2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4A4
-
-
?
prostaglandin A2 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin A2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4A6
-
-
?
prostaglandin A2 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin A2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4A7
-
-
?
quinine + [reduced NADPH-hemoprotein reductase] + O2
3-hydroxyquinine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
quinine + [reduced NADPH-hemoprotein reductase] + O2
3-hydroxyquinine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
quinine + [reduced NADPH-hemoprotein reductase] + O2
3-hydroxyquinine + [oxidized NADPH-hemoprotein reductase] + H2O
-
in the microsomal membranes, CYP3A4 interacts with the NADPH-P450 reductase to receive electrons used in metabolism of drugs and xenobiotics. The heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions
-
-
?
RH + [reduced NADPH-hemoprotein reductase] + O2
ROH + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
RH + [reduced NADPH-hemoprotein reductase] + O2
ROH + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
RH + [reduced NADPH-hemoprotein reductase] + O2
ROH + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
sertraline + [reduced NADPH-hemoprotein reductase] + O2
demethylsertraline + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
i.e. (1S,4S)-N-methyl-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydro-1-naphthylamine, a one-step oxidative N-demethylation
-
-
?
sertraline + [reduced NADPH-hemoprotein reductase] + O2
demethylsertraline + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
i.e. (1S,4S)-N-methyl-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydro-1-naphthylamine, a one-step oxidative N-demethylation
-
-
?
testosterone + [reduced NADPH-hemoprotein reductase] + O2
6beta-hydroxytestosterone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
testosterone + [reduced NADPH-hemoprotein reductase] + O2
6beta-hydroxytestosterone + [oxidized NADPH-hemoprotein reductase] + H2O
CYP3A4
-
-
?
testosterone + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
testosterone + [reduced NADPH-hemoprotein reductase] + O2
?
CYP3A4
-
-
?
tetralin + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-tetralin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
tetralin + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-tetralin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
tolbutamide + [reduced NADPH-hemoprotein reductase] + O2
?
CYP2C9
-
-
?
tolbutamide + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
xanthotoxin + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
-
-
-
-
?
xanthotoxin + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
-
-
-
?
additional information
?
-
no activity with valencene, beta-caryophyllene, ledene, gurjunene, farnesene, epdicedrol, artemisinic acid, arteannulin B, artemisinin, dihydroartemisinic acid, norannuic acid, myristic acid, and palmitic acid
-
-
?
additional information
?
-
-
no activity with valencene, beta-caryophyllene, ledene, gurjunene, farnesene, epdicedrol, artemisinic acid, arteannulin B, artemisinin, dihydroartemisinic acid, norannuic acid, myristic acid, and palmitic acid
-
-
?
additional information
?
-
-
the enzyme catalyzes oxidation of methanol, acetone, dimethylsulfoxide, n-hexadecane, n-octadecane, and naphthalene
-
-
?
additional information
?
-
-
the enzyme catalyzes oxidation of methanol, acetone, dimethylsulfoxide, n-hexadecane, n-octadecane, and naphthalene
-
-
?
additional information
?
-
-
CYP102A7 is active towards medium-chain fatty acids but shows a strong preference for saturated over unsaturated fatty acids. Besides fatty acids, CYP102A7 is able to catalyse the oxidation of cyclic and acyclic terpenes with high activity and coupling efficiency. 7-methoxycoumarin is not converted by CYP102A7. No NADPH consumption with 11-deoxycortisol, dextromethorphane, testosterone and cyclic and acyclic alkanes as substrates
-
-
?
additional information
?
-
-
CYP102A7 is active towards medium-chain fatty acids but shows a strong preference for saturated over unsaturated fatty acids. Besides fatty acids, CYP102A7 is able to catalyse the oxidation of cyclic and acyclic terpenes with high activity and coupling efficiency. 7-methoxycoumarin is not converted by CYP102A7. No NADPH consumption with 11-deoxycortisol, dextromethorphane, testosterone and cyclic and acyclic alkanes as substrates
-
-
?
additional information
?
-
-
activity involves cytochrome c reduction, CYP102A3 hydroxylates and epoxidizes middle to long chain saturated, unsaturated and branched fatty acids at subterminal positions
-
-
?
additional information
?
-
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview, the enzyme bridges the clavine and ergoline alkaloid pathways, it is critical in the ergot alkaloid gene cluster
-
-
?
additional information
?
-
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview
-
-
?
additional information
?
-
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview, the enzyme bridges the clavine and ergoline alkaloid pathways, it is critical in the ergot alkaloid gene cluster
-
-
?
additional information
?
-
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview
-
-
?
additional information
?
-
-
no substrate: chloropropham, quizalofopethyl, isoxaben
-
-
?
additional information
?
-
-
a xenobiotic-metabolizing cytochrome P450 monooxygenase that contributes extensively to drug and toxin metabolism, CYP3A4 is the predominant enzyme in the clearance of about 50% of therapeutic drugs
-
-
?
additional information
?
-
-
in humans, CYP3A4 appears to be the dominant CYP and contributes to over 60% of the metabolism of drugs, the Ah receptor is important in CYP1A1 regulation, a number of mechanisms occur to regulate CYP including enhancement of mRNA stability, modulation of heme degradation, enzyme phosphorylation, and protein-protein interactions
-
-
?
additional information
?
-
-
the cytochrome P-450 4, CYP4, family catalyze the omega-hydroxylation of fatty acids, metabolic regulation, overview
-
-
?
additional information
?
-
-
CYP mainly catalyzes C-H abstraction but also oxidizes nitrogen- and sulfur-containing compounds and generally converts lipophilic compounds into more hydrophilic metabolites
-
-
?
additional information
?
-
-
substrates bind in a cavity above the heme surface, function-structure relationship, the outer surfaces of the active site cavity are formed by portions of beta-sheets 1 and 4, helices FG, and the loop between helices B and C, overview
-
-
?
additional information
?
-
-
CYP2C19 can not form fenthion-oxon-sulfoxide from fenthion-oxon
-
-
?
additional information
?
-
CYP2C19 can not form fenthion-oxon-sulfoxide from fenthion-oxon
-
-
?
additional information
?
-
CYP2C19 can not form fenthion-oxon-sulfoxide from fenthion-oxon
-
-
?
additional information
?
-
CYP2C19 can not form fenthion-oxon-sulfoxide from fenthion-oxon
-
-
?
additional information
?
-
CYP2C19 can not form fenthion-oxon-sulfoxide from fenthion-oxon
-
-
?
additional information
?
-
CYP2C19 can not form fenthion-oxon-sulfoxide from fenthion-oxon
-
-
?
additional information
?
-
-
reacts with activity-based proteins of varying chemical composition, quite distinct from their natural substrates
-
-
?
additional information
?
-
-
CYP4A enzymes predominantly function as AA omega-hydroxylases, hydroxy metabolites are roduced by the individual CYP isoforms in a regio- and stereoselective manner. CYP isoforms that do not produce 20-hydroxyeicosatetraenoic acid but function predominantly as AA (omega-1)-hydroxylases include CYP1A1, but also act regioselective
-
-
?
additional information
?
-
-
CYP1A2 catalyzes the O-demethylation of 7-methoxyresorufin
-
-
?
additional information
?
-
-
the enzyme shows (omega-1)-hydroxylase activity against arachidonic acid, linoleic acid, and especially against eicosapentaenoic acid and docosahexaenoic acid, substrate specificities of isozymes, overview
-
-
?
additional information
?
-
-
(1R)-trans-permethrin is the best substrate among the permethrin enantiomers
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
-
effect of toxification on hepaic metabolism and biotransformation enzyme levels, overview
-
-
?
additional information
?
-
-
effect of toxification on hepatic metabolism and biotransformation enzyme levels, overview
-
-
?
additional information
?
-
the concomitant down-regulation of P450arom and up-regulation of P45011beta are of pivotal importance to the sex change
-
-
?
additional information
?
-
-
the concomitant down-regulation of P450arom and up-regulation of P45011beta are of pivotal importance to the sex change
-
-
?
additional information
?
-
-
CYP4A enzymes predominantly function as AA omega-hydroxylases, hydroxy metabolites are roduced by the individual CYP isoforms in a regio- and stereoselective manner. CYP isoforms that do not produce 20-hydroxyeicosatetraenoic acid but function predominantly as AA (omega-1)-hydroxylases include CYP1A1, but also act regioselective
-
-
?
additional information
?
-
-
the enzyme shows (omega-1)-hydroxylase activity against arachidonic acid, linoleic acid, and especially against eicosapentaenoic acid and docosahexaenoic acid, substrate specificities of isozymes, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
?
additional information
?
-
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
?
additional information
?
-
Q38Q86
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
?
additional information
?
-
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
?
additional information
?
-
-
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
?
additional information
?
-
the enzyme demethylates nicotine to nornicotine
-
-
?
additional information
?
-
the enzyme demethylates nicotine to nornicotine
-
-
?
additional information
?
-
Q38Q86
the enzyme demethylates nicotine to nornicotine
-
-
?
additional information
?
-
the enzyme demethylates nicotine to nornicotine
-
-
?
additional information
?
-
-
the enzyme demethylates nicotine to nornicotine
-
-
?
additional information
?
-
-
no activity with prostaglandins of E type, CYP4A6
-
-
?
additional information
?
-
-
no activity with prostaglandins of E type, CYP4A7
-
-
?
additional information
?
-
-
regiospecific and stereo-specific activity, overview
-
-
?
additional information
?
-
-
CYP1A2 cooperates with NADPH-cytochrome P450 reductase, CPR. Differential sensitivity of CPR binding to CYP1A2 depending on the substrate present, overview
-
-
?
additional information
?
-
EUI acts as a gibberellic acid inactivating enzyme, in eui mutant plans, the biological activity of GA4 is reduced, expression of Eui is tightly regulated during plant development with the stage-specific eui phenotypes, GA biosynthesis and catabolism pathways, overview, the enzyme negatively regulates gibberellic acid metabolism, mechanism, overview
-
-
?
additional information
?
-
-
EUI acts as a gibberellic acid inactivating enzyme, in eui mutant plans, the biological activity of GA4 is reduced, expression of Eui is tightly regulated during plant development with the stage-specific eui phenotypes, GA biosynthesis and catabolism pathways, overview, the enzyme negatively regulates gibberellic acid metabolism, mechanism, overview
-
-
?
additional information
?
-
EUI catalyzes the 16alpha,17-epoxidation of non-13-hydroxylated gibberellic acids with very high activity on giberellic acid GA4, substrate specificity, overview, no activity with the 13-hydroxylated GA1, GA20, and GA53
-
-
?
additional information
?
-
-
EUI catalyzes the 16alpha,17-epoxidation of non-13-hydroxylated gibberellic acids with very high activity on giberellic acid GA4, substrate specificity, overview, no activity with the 13-hydroxylated GA1, GA20, and GA53
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of astaxanthin, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of astaxanthin, overview
-
-
?
additional information
?
-
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
-
no activity with fluorene, anthracene, phenanthrene, and acenaphthene
-
-
?
additional information
?
-
-
the enzyme also acts as an alkane-hydroxylase that oxidizes n-alkanes with various chain lengths (C9to C12and C15to C19), as well as alkyl side chains (C3to C9) in alkylphenols. CYP63A2 shows preferential oxidation of long-chain alkylphenols and alkanes
-
-
?
additional information
?
-
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
-
no reaction with trans-stilbene
-
-
?
additional information
?
-
-
no reaction with trans-stilbene
-
-
?
additional information
?
-
-
self-sufficient fatty acid monooxygenase
-
-
?
additional information
?
-
-
enzyme catalyses hydroxylation in the omega-1, omega-2 and omega-3 positions and/or epoxidation of medium- and long-chain fatty acids
-
-
?
additional information
?
-
-
activity involves cytochrome c reduction, CYP102A1 hydroxylates and epoxidizes middle to long chain saturated, unsaturated and branched fatty acids at subterminal positions, an engineered CYP102A1 heme domain which utilizes H2O2 as electron donor
-
-
?
additional information
?
-
wild type CYP102A1 has no oxidizing activity toward ()-alpha- and ()-beta-pinene
-
-
?
additional information
?
-
-
wild type CYP102A1 has no oxidizing activity toward ()-alpha- and ()-beta-pinene
-
-
?
additional information
?
-
-
no fluctuations between the light and dark periods under ad libitum and restricted feeding conditions, effects on P450 monooxygenase activities in male rats, overview
-
-
?
additional information
?
-
-
the cytochrome P-450 4, CYP4, family catalyze the omega-hydroxylation of fatty acids, metabolic regulation, overview, PPARalpha agonist increased the transcription activity of rat CYP4A1
-
-
?
additional information
?
-
-
the enzyme performs dealkylation of 7-alkoxycoumarin
-
-
?
additional information
?
-
-
CYP4A enzymes predominantly function as AA omega-hydroxylases, hydroxy metabolites are roduced by the individual CYP isoforms in a regio- and stereoselective manner. CYP isoforms that do not produce 20-hydroxyeicosatetraenoic acid but function predominantly as AA (omega-1)-hydroxylases include CYP1A1, but also act regioselective
-
-
?
additional information
?
-
-
the enzyme shows (omega-1)-hydroxylase activity against arachidonic acid, linoleic acid, and especially against eicosapentaenoic acid and docosahexaenoic acid, substrate specificities of isozymes, overview
-
-
?
additional information
?
-
-
no activity with anthraquinone-1,8-disulfonic acid
-
-
?
additional information
?
-
product identifications, no activity with alpha-pinene, terpeneol, ethoxyresorufin, and cyclohexane, a natural self-sufficient fusion protein consisting of ferredoxin, flavin-containing reductase, and P450 monooxygenase, substrate specificity: in the presence of NADPH, the enzyme shows hydroxylation activity towards polycyclic aromatic hydrocarbons naphthalene, indene, acenaphthene, toluene, fluorene, m-xylene, and ethyl benzene, the conversion of naphthalene, acenaphthene, and fluorene results in respective ring monohydroxylated metabolites, alkyl aromatics like toluene, m-xylene, and ethyl benzene are hydroxylated exclusively at the side chains
-
-
?
additional information
?
-
-
product identifications, no activity with alpha-pinene, terpeneol, ethoxyresorufin, and cyclohexane, a natural self-sufficient fusion protein consisting of ferredoxin, flavin-containing reductase, and P450 monooxygenase, substrate specificity: in the presence of NADPH, the enzyme shows hydroxylation activity towards polycyclic aromatic hydrocarbons naphthalene, indene, acenaphthene, toluene, fluorene, m-xylene, and ethyl benzene, the conversion of naphthalene, acenaphthene, and fluorene results in respective ring monohydroxylated metabolites, alkyl aromatics like toluene, m-xylene, and ethyl benzene are hydroxylated exclusively at the side chains
-
-
?
additional information
?
-
-
YP116B3 catalyzes the dealkylation of 7-ethoxycoumarin and the hydroxylation of substituted and unsubstituted aromatics, overview
-
-
?
additional information
?
-
-
no hydroxylation activity towards naphthalene, indene, ethyl benzene, and m-xylene
-
-
?
additional information
?
-
Roseibium aggregatum
versatile catalyst, exhibiting hydroxylation and epoxidation activities as well as O-dealkylation and asymmetric sulfoxidation activities. Alkylbenzenes, aromatic bicyclic molecules, and terpenoids are hydroxylated by Cyp116B4
-
-
?
additional information
?
-
Roseibium aggregatum DSM 13394
versatile catalyst, exhibiting hydroxylation and epoxidation activities as well as O-dealkylation and asymmetric sulfoxidation activities. Alkylbenzenes, aromatic bicyclic molecules, and terpenoids are hydroxylated by Cyp116B4
-
-
?
additional information
?
-
isoform Sam5 hydroxylates isoflavones, flavanones, and flavones but does not produce any detectable hydroxylated product with flavonols. Naringenin is the most preferred substrate, followed by eriodictyol, genistein,apigenin, luteolin, and daidzein
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
Sorghum sp.
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
-
palmitate, stearate, and oleate show negligible binding to isoform CYP102B1, in contrast to CYP102A1
-
-
?
additional information
?
-
-
palmitate, stearate, and oleate show negligible binding to isoform CYP102B1, in contrast to CYP102A1
-
-
?
additional information
?
-
-
the enzyme is involved in macrolide biosynthesis and performs unusual C4-hydroxylation
-
-
?
additional information
?
-
-
structural diversification of macrolactones by the substrate-flexible enzyme, substrate specificity, degree of plasticity towards alternative substrates, overview, modeling of macrolide conformations and enzyme-substrate complex
-
-
?
additional information
?
-
-
no activity with 3-acetylindole
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-(methylnitrosamino)-1-(3pyridyl)-1-butanone + [reduced NADPH-hemoprotein reductase] + O2
?
-
nicotine oxidase activity of CYP2A6, activates the tobacco-derived carcinogens to mutagenic products
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
7-methoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + ?
-
-
-
-
?
aflatoxin B1 + [reduced NADPH-hemoprotein reductase] + O2
?
-
i.e. AFB1, bioactivation of the carcinogenic mycotoxin to a toxic compound, although not acutely toxic at low concentrations, AFB1 had significant chronic effects, including protracted development, increased mortality, decreased pupation rate, and reduced pupal weight, sensitivity varies with developmental stage, whereas intermediate concentrations causes complete mortality in first instars, this same concentration has no detectable adverse effects on larvae encountering AFB1 in fifth instar. These compounds owe their toxicity to their ability to form irreversible adducts to nucleic acids with the concomitant inhibition of DNA replication and DNA-dependent transcription, mortality, overview
-
-
?
aminopyrine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
avermectin + [reduced NADPH-hemoprotein reductase] + O2
4''-oxo-avermectin + [oxidized NADPH-hemoprotein reductase] + H2O
bentazon + [reduced NADPH-hemoprotein reductase] + O2
?
-
ring-hydroxylation
-
-
?
benzo-pyrene + [reduced NADPH-hemoprotein reductase] + O2
?
-
recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
diclofop + [reduced NADPH-hemoprotein reductase] + O2
?
-
ring-hydroxylation
-
-
?
elymoclavine + [reduced NADPH-hemoprotein reductase] + O2
paspalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
giberellic acid GA4 + [reduced NADPH-hemoprotein reductase] + O2
16alpha,17-epoxy GA4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
the product is transformed further to 16,17-dihydro-16alpha,17-dihydroxy-GA4 in the plant
-
?
indane + [reduced NADPH-hemoprotein reductase] + O2
(S)-3-hydroxy-indane + [oxidized NADPH-hemoprotein reductase] + H2O
macrolide YC-17 + [reduced NADPH-hemoprotein reductase] + O2
methymycin + [oxidized NADPH-hemoprotein reductase] + H2O
-
Hydroxylation of C-10 position yield methymycin and of the C-12 neomethymycin. Hydroxylation at both positions yields novamethymycin.
-
-
?
macrolide YC-17 + [reduced NADPH-hemoprotein reductase] + O2
neomethymycin + [oxidized NADPH-hemoprotein reductase] + H2O
-
Hydroxylation of C-10 position yield methymycin and of the C-12 neomethymycin. Hydroxylation at both positions yields novamethymycin.
-
-
?
macrolide YC-17 + [reduced NADPH-hemoprotein reductase] + O2
novamethymycin + [oxidized NADPH-hemoprotein reductase] + H2O
-
Hydroxylation of C-10 position yield methymycin and of the C-12 neomethymycin. Hydroxylation at both positions yields novamethymycin.
-
-
?
metolachlor + [reduced NADPH-hemoprotein reductase] + O2
?
Sorghum sp.
-
de-ethylation
-
-
?
N'-nitrosonornicotine + [reduced NADPH-hemoprotein reductase] + O2
?
-
nicotine oxidase activity of CYP2A6, activates the tobacco-derived carcinogens to mutagenic products
-
-
?
narbomycin + [reduced NADPH-hemoprotein reductase] + O2
pikromycin + [oxidized NADPH-hemoprotein reductase] + H2O
-
the organism is a pikromycin producer
-
-
?
prostaglandin + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-prostaglandin + [oxidized NADPH-hemoprotein reductase] + H2O
-
physiological functions are the metabolic inactivation of prostaglandins and the production of 20-hydroxyeicosatetraenoic acid, CYP4A4
-
-
?
quinine + [reduced NADPH-hemoprotein reductase] + O2
3-hydroxyquinine + [oxidized NADPH-hemoprotein reductase] + H2O
-
in the microsomal membranes, CYP3A4 interacts with the NADPH-P450 reductase to receive electrons used in metabolism of drugs and xenobiotics. The heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions
-
-
?
RH + [reduced NADPH-hemoprotein reductase] + O2
ROH + [oxidized NADPH-hemoprotein reductase] + H2O
sertraline + [reduced NADPH-hemoprotein reductase] + O2
demethylsertraline + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
tetralin + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-tetralin + [oxidized NADPH-hemoprotein reductase] + H2O
additional information
?
-
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
-
wild-type enzyme and recombinant enzyme P4502B6 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
-
wild-type enzyme and recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
-
-
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxycoumarin O-deethylation
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxycoumarin O-deethylation
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxycoumarin O-deethylation
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxyresorufin O-deethylation
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxyresorufin O-deethylation
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
-
7-ethoxyresorufin O-deethylation
-
-
?
aminopyrine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
aminopyrene-N-demethylation
-
-
?
aminopyrine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
aminopyrene-N-demethylation
-
-
?
aminopyrine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
aminopyrene-N-demethylation
-
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
-
-
i.e. 20-HETE, a potent constrictor of renal microvessels and inhibits Na+ reabsorption in the proximal tubule and thick ascending limb
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
-
-
i.e. 20-HETE, a potent constrictor of renal microvessels and inhibits Na+ reabsorption in the proximal tubule and thick ascending limb
-
?
avermectin + [reduced NADPH-hemoprotein reductase] + O2
4''-oxo-avermectin + [oxidized NADPH-hemoprotein reductase] + H2O
-
4''-oxo-avermectin is a key intermediate in the manufacture of the agriculturally important insecticide emamectin benzoate from the natural product avermectin, overview
-
-
?
avermectin + [reduced NADPH-hemoprotein reductase] + O2
4''-oxo-avermectin + [oxidized NADPH-hemoprotein reductase] + H2O
-
4''-oxo-avermectin is a key intermediate in the manufacture of the agriculturally important insecticide emamectin benzoate from the natural product avermectin, overview
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
recombinant wild-type enzyme and enzyme mutant fused to yeast reductase expressed in transgenic potato plants
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
ring methyl-hydroxylation
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group, recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
-
ring methyl-hydroxylation
-
-
?
elymoclavine + [reduced NADPH-hemoprotein reductase] + O2
paspalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
the product is the precursor for D-lysergic acid
-
?
elymoclavine + [reduced NADPH-hemoprotein reductase] + O2
paspalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
the product is the precursor for D-lysergic acid
-
?
indane + [reduced NADPH-hemoprotein reductase] + O2
(S)-3-hydroxy-indane + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
indane + [reduced NADPH-hemoprotein reductase] + O2
(S)-3-hydroxy-indane + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
RH + [reduced NADPH-hemoprotein reductase] + O2
ROH + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
RH + [reduced NADPH-hemoprotein reductase] + O2
ROH + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
RH + [reduced NADPH-hemoprotein reductase] + O2
ROH + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
sertraline + [reduced NADPH-hemoprotein reductase] + O2
demethylsertraline + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
i.e. (1S,4S)-N-methyl-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydro-1-naphthylamine, a one-step oxidative N-demethylation
-
-
?
sertraline + [reduced NADPH-hemoprotein reductase] + O2
demethylsertraline + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
i.e. (1S,4S)-N-methyl-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydro-1-naphthylamine, a one-step oxidative N-demethylation
-
-
?
tetralin + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-tetralin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
tetralin + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxy-tetralin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
?
-
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview, the enzyme bridges the clavine and ergoline alkaloid pathways, it is critical in the ergot alkaloid gene cluster
-
-
?
additional information
?
-
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview, the enzyme bridges the clavine and ergoline alkaloid pathways, it is critical in the ergot alkaloid gene cluster
-
-
?
additional information
?
-
-
a xenobiotic-metabolizing cytochrome P450 monooxygenase that contributes extensively to drug and toxin metabolism, CYP3A4 is the predominant enzyme in the clearance of about 50% of therapeutic drugs
-
-
?
additional information
?
-
-
in humans, CYP3A4 appears to be the dominant CYP and contributes to over 60% of the metabolism of drugs, the Ah receptor is important in CYP1A1 regulation, a number of mechanisms occur to regulate CYP including enhancement of mRNA stability, modulation of heme degradation, enzyme phosphorylation, and protein-protein interactions
-
-
?
additional information
?
-
-
the cytochrome P-450 4, CYP4, family catalyze the omega-hydroxylation of fatty acids, metabolic regulation, overview
-
-
?
additional information
?
-
-
CYP4A enzymes predominantly function as AA omega-hydroxylases, hydroxy metabolites are roduced by the individual CYP isoforms in a regio- and stereoselective manner. CYP isoforms that do not produce 20-hydroxyeicosatetraenoic acid but function predominantly as AA (omega-1)-hydroxylases include CYP1A1, but also act regioselective
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
-
effect of toxification on hepaic metabolism and biotransformation enzyme levels, overview
-
-
?
additional information
?
-
-
effect of toxification on hepatic metabolism and biotransformation enzyme levels, overview
-
-
?
additional information
?
-
the concomitant down-regulation of P450arom and up-regulation of P45011beta are of pivotal importance to the sex change
-
-
?
additional information
?
-
-
the concomitant down-regulation of P450arom and up-regulation of P45011beta are of pivotal importance to the sex change
-
-
?
additional information
?
-
-
CYP4A enzymes predominantly function as AA omega-hydroxylases, hydroxy metabolites are roduced by the individual CYP isoforms in a regio- and stereoselective manner. CYP isoforms that do not produce 20-hydroxyeicosatetraenoic acid but function predominantly as AA (omega-1)-hydroxylases include CYP1A1, but also act regioselective
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
?
additional information
?
-
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
?
additional information
?
-
Q38Q86
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
?
additional information
?
-
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
?
additional information
?
-
-
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
?
additional information
?
-
EUI acts as a gibberellic acid inactivating enzyme, in eui mutant plans, the biological activity of GA4 is reduced, expression of Eui is tightly regulated during plant development with the stage-specific eui phenotypes, GA biosynthesis and catabolism pathways, overview, the enzyme negatively regulates gibberellic acid metabolism, mechanism, overview
-
-
?
additional information
?
-
-
EUI acts as a gibberellic acid inactivating enzyme, in eui mutant plans, the biological activity of GA4 is reduced, expression of Eui is tightly regulated during plant development with the stage-specific eui phenotypes, GA biosynthesis and catabolism pathways, overview, the enzyme negatively regulates gibberellic acid metabolism, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of astaxanthin, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of astaxanthin, overview
-
-
?
additional information
?
-
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
-
no fluctuations between the light and dark periods under ad libitum and restricted feeding conditions, effects on P450 monooxygenase activities in male rats, overview
-
-
?
additional information
?
-
-
the cytochrome P-450 4, CYP4, family catalyze the omega-hydroxylation of fatty acids, metabolic regulation, overview, PPARalpha agonist increased the transcription activity of rat CYP4A1
-
-
?
additional information
?
-
-
CYP4A enzymes predominantly function as AA omega-hydroxylases, hydroxy metabolites are roduced by the individual CYP isoforms in a regio- and stereoselective manner. CYP isoforms that do not produce 20-hydroxyeicosatetraenoic acid but function predominantly as AA (omega-1)-hydroxylases include CYP1A1, but also act regioselective
-
-
?
additional information
?
-
-
YP116B3 catalyzes the dealkylation of 7-ethoxycoumarin and the hydroxylation of substituted and unsubstituted aromatics, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
Sorghum sp.
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
-
the enzyme is involved in macrolide biosynthesis and performs unusual C4-hydroxylation
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
?
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Lang, M.A.; Nebert, D.W.
Structural gene products of the Ah locus. Evidence for many unique P-450-mediated monooxygenase activities reconstituted from 3-methylcholanthrene-treated C57BL/6N mouse liver microsomes
J. Biol. Chem.
256
12058-12067
1981
Mus musculus
brenda
Lang, M.A.; Gielen, J.E.; Nebert, D.W.
Genetic evidence for many unique liver microsomal P-450-mediated monooxygenase activities in heterogeneic stock mice
J. Biol. Chem.
256
12068-12075
1981
Mus musculus
brenda
Theoharides, A.D.; Kupfer, D.
Evidence for different hepatic microsomal monooxygenases catalyzing omega- and (omega-1)-hydroxylations of prostaglandins E1 and E2. Effects of inducers of monooxygenase on the kinetic constants of prostaglandin hydroxylation
J. Biol. Chem.
256
2168-2175
1981
Rattus norvegicus
brenda
Oliver, C.F.; Modi, S.; Primrose, W.U.; Lian, L.Y.; Roberts, G.C.K.
Engineering the substrate specificity of Bacillus megaterium cytochrome P-450 BM3: hydroxylation of alkyl trimethylammonium compounds
Biochem. J.
327
537-544
1997
Priestia megaterium
-
brenda
Sevrioukova, I.F.; Li, H.; Zhang, H.; Peterson, J.A.; Poulos, T.L.
Structure of a cytochrome P450-redox partner electron-transfer complex
Proc. Natl. Acad. Sci. USA
96
1863-1868
1999
Priestia megaterium
brenda
Eschenfeldt, W.H.; Zhang, Y.; Samaha, H.; Stols, L.; Eirich, L.D.; Wilson, C.R.; Donnelly, M.I.
Transformation of fatty acids catalyzed by cytochrome P450 monooxygenase enzymes of Candida tropicalis
Appl. Environ. Microbiol.
69
5992-5999
2003
Candida tropicalis
brenda
Gewonyo, K.; Buckland, B.C.; Lilly, M.D.
Development of a large-scale continuous substrate to feed process for the biotransformation of simvastatin by Nocardia sp.
Biotechnol. Bioeng.
37
1101-1107
1991
Pseudonocardia autotrophica
brenda
Cashman, J.R.; Lattard, V.; Lin, J.
Effect of total parenteral nutrition and choline on hepatic flavin-containing and cytochrome P-450 monooxygenase activity in rats
Drug Metab. Dispos.
32
222-229
2004
Rattus norvegicus
brenda
Chen, J.S.; Berenbaum, M.R.; Schuler, M.A.
Amino acids in SRS1 and SRS6 are critical for furanocoumarin metabolism by CYP6B1v1, a cytochrome P450 monooxygenase
Insect Mol. Biol.
11
175-186
2002
Papilio polyxenes (Q04552), Papilio polyxenes
brenda
Hirose, S.; Kawahigashi, H.; Ozawa, K.; Shiota, N.; Inui, H.; Ohkawa, H.; Ohkawa, Y.
Transgenic rice containing human CYP2B6 detoxifies various classes of herbicides
J. Agric. Food Chem.
53
3461-3467
2005
Homo sapiens
brenda
Lentz, O.; Urlacher, V.; Schmid, R.D.
Substrate specificity of native and mutated cytochrome P450 (CYP102A3) from Bacillus subtilis
J. Biotechnol.
108
41-49
2004
Bacillus subtilis
brenda
Kikuta, Y.; Kusunose, E.; Kusunose, M.
Prostaglandin and leukotriene omega-hydroxylases
Prostaglandins
68-69
345-362
2002
Oryctolagus cuniculus
brenda
Baudry, J.; Li, W.; Pan, L.; Berenbaum, M.R.; Schuler, M.A.
Molecular docking of substrates and inhibitors in the catalytic site of CYP6B1, an insect cytochrome P450 monooxygenase
Protein Eng.
16
577-587
2003
Papilio polyxenes
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Lee, S.K.; Basnet, D.B.; Hong, J.S.; Jung, W.S.; Choi, C.Y.; Lee, H.C.; Sohng, J.K.; Ryu, K.G.; Kim, D.J.; Ahn, J.S.; Kim, B.S.; Oh, H.C.; Sherman, D.H.; Yoon, Y.J.
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Henczova, M.; Deer, A.K.; Komlosi, V.; Mink, J.
Detection of toxic effects of Cd(2+) on different fish species via liver cytochrome P450-dependent monooxygenase activities and FTIR spectroscopy
Anal. Bioanal. Chem.
385
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Cyprinus carpio, Silurus glanis, Hypophthalmichthys molitrix
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Jungmann, V.; Molnar, I.; Hammer, P.E.; Hill, D.S.; Zirkle, R.; Buckel, T.G.; Buckel, D.; Ligon, J.M.; Pachlatko, J.P.
Biocatalytic conversion of avermectin to 4"-oxo-avermectin: characterization of biocatalytically active bacterial strains and of cytochrome p450 monooxygenase enzymes and their genes
Appl. Environ. Microbiol.
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Liu, L.; Schmid, R.D.; Urlacher, V.B.
Cloning, expression, and characterization of a self-sufficient cytochrome P450 monooxygenase from Rhodococcus ruber DSM 44319
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Rhodococcus ruber (Q52TE7), Rhodococcus ruber
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Johnson, E.F.; Stout, C.D.
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Homo sapiens
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Cashman, J.R.
Some distinctions between flavin-containing and cytochrome P450 monooxygenases
Biochem. Biophys. Res. Commun.
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Homo sapiens
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Roccatano, D.; Wong, T.S.; Schwaneberg, U.; Zacharias, M.
Toward understanding the inactivation mechanism of monooxygenase P450 BM-3 by organic cosolvents: a molecular dynamics simulation study
Biopolymers
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2006
Priestia megaterium (P14779), Priestia megaterium
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Vatsyayan, P.; Kumar, A.K.; Goswami, P.; Goswami, P.
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Biores. Technol.
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brenda
Gorinova, N.; Nedkovska, M.; Atanassov, A.
Cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants
Biotechnol. Biotechnol. Equip.
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Homo sapiens, Lolium rigidum, Nicotiana tabacum, Phelipanche ramosa, Rattus norvegicus, Solanum tuberosum, Sorghum sp., Triticum aestivum, Zea mays
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Doddapaneni, H.; Chakraborty, R.; Yadav, J.S.
Genome-wide structural and evolutionary analysis of the P450 monooxygenase genes (P450ome) in the white rot fungus Phanerochaete chrysosporium: Evidence for gene duplications and extensive gene clustering
BMC Genomics
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Phanerodontia chrysosporium, Phanerodontia chrysosporium (Q4G2S1), Phanerodontia chrysosporium (Q4G2S2), Phanerodontia chrysosporium (Q4G2S3), Phanerodontia chrysosporium (Q4L230), Phanerodontia chrysosporium (Q4L231), Phanerodontia chrysosporium BKM-F-1767, Phanerodontia chrysosporium BKM-F-1767 (Q4G2S1), Phanerodontia chrysosporium BKM-F-1767 (Q4G2S2), Phanerodontia chrysosporium BKM-F-1767 (Q4G2S3), Phanerodontia chrysosporium BKM-F-1767 (Q4L230), Phanerodontia chrysosporium BKM-F-1767 (Q4L231)
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Identification of the cytochrome P450 monooxygenase that bridges the clavine and ergoline alkaloid pathways
Chembiochem
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Arun, S.; Rajendran, A.; Subramanian, P.
Subcellular/tissue distribution and responses to oil exposure of the cytochrome P450-dependent monooxygenase system and glutathione S-transferase in freshwater prawns (Macrobrachium malcolmsonii, M. lamarrei lamarrei)
Ecotoxicology
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Macrobrachium lamarrei, Macrobrachium malcolmsonii
brenda
Chan, P.K.; Lu, S.Y.; Liao, J.W.; Wei, C.F.; Tsai, Y.; Ueng, T.H.
Induction and inhibition of cytochrome P450-dependent monooxygenases of rats by fungicide bitertanol
Food Chem. Toxicol.
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Rattus norvegicus
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The crtS gene of Xanthophyllomyces dendrorhous encodes a novel cytochrome-P450 hydroxylase involved in the conversion of beta-carotene into astaxanthin and other xanthophylls
Fungal Genet. Biol.
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Phaffia rhodozyma
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Structure of microsomal cytochrome P450 2B4 complexed with the antifungal drug bifonazole: insight into P450 conformational plasticity and membrane interaction
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Homo sapiens, Rattus norvegicus
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Yun, M.; Yogo, Y.; Miura, R.; Yamasue, Y.; Fischer, A.J.
Cytochrome P-450 monooxygenase activity in herbicide-resistant and -susceptible late watergrass (Echinochloa phyllopogon)
Pestic. Biochem. Physiol.
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Echinochloa phyllopogon
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Zhu, Y.; Nomura, T.; Xu, Y.; Zhang, Y.; Peng, Y.; Mao, B.; Hanada, A.; Zhou, H.; Wang, R.; Li, P.; Zhu, X.; Mander, L.N.; Kamiya, Y.; Yamaguchi, S.; He, Z.
Elongated uppermost internode encodes a cytochrome P450 monooxygenase that epoxidizes gibberellins in a novel deactivation reaction in rice
Plant Cell
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Oryza sativa (Q5KQH7), Oryza sativa
brenda
Siminszky, B.; Gavilano, L.; Bowen, S.W.; Dewey, R.E.
Conversion of nicotine to nornicotine in Nicotiana tabacum is mediated by CYP82E4, a cytochrome P450 monooxygenase
Proc. Natl. Acad. Sci. USA
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Nicotiana tabacum (Q38Q84), Nicotiana tabacum (Q38Q85), Nicotiana tabacum (Q38Q86), Nicotiana tabacum (Q38Q87), Nicotiana tabacum
brenda
Kranendonk, M.; Marohnic, C.C.; Panda, S.P.; Duarte, M.P.; Oliveira, J.S.; Masters, B.S.; Rueff, J.
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Homo sapiens
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Effects of Cu(2+) and Pb(2+) on different fish species: liver cytochrome P450-dependent monooxygenase activities and FTIR spectra
Comp. Biochem. Physiol. C
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Cyprinus carpio, Silurus glanis, Hypophthalmichthys molitrix
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Panicco, P.; Astuti, Y.; Fantuzzi, A.; Durrant, J.R.; Gilardi, G.
P450 versus P420: Correlation between Cyclic Voltammetry and Visible Absorption Spectroscopy of the Immobilized Heme Domain of Cytochrome P450 BM3
J. Phys. Chem. B
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Branco, R.J.; Seifert, A.; Budde, M.; Urlacher, V.B.; Ramos, M.J.; Pleiss, J.
Anchoring effects in a wide binding pocket: The molecular basis of regioselectivity in engineered cytochrome P450 monooxygenase from B. megaterium
Proteins
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Priestia megaterium (P14779), Priestia megaterium
brenda
Liu, J.F.; Guiguen, Y.; Liu, S.J.
Aromatase (P450arom) and 11beta-hydroxylase (P45011beta) genes are differentially expressed during the sex change process of the protogynous rice field eel, Monopterus albus
Fish Physiol. Biochem.
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Monopterus albus (Q2I129), Monopterus albus
brenda
Pachecka, J.; Tomaszewski, P.; Kubiak-Tomaszewska, G.
Cytochrome P450 polymorphism--molecular, metabolic and pharmacogenetic aspects. I. Mechanisms of activity of cytochrome P450 monooxygenases
Acta Pol. Pharm.
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Homo sapiens
brenda
Subramanian, V.; Yadav, J.S.
Role of P450 monooxygenases in the degradation of the endocrine-disrupting chemical nonylphenol by the white rot fungus Phanerochaete chrysosporium
Appl. Environ. Microbiol.
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Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Dietrich, M.; Eiben, S.; Asta, C.; Do, T.A.; Pleiss, J.; Urlacher, V.B.
Cloning, expression and characterisation of CYP102A7, a self-sufficient P450 monooxygenase from Bacillus licheniformis
Appl. Microbiol. Biotechnol.
79
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Bacillus licheniformis, Bacillus licheniformis DSM 13
brenda
Zhang, J.D.; Li, A.T.; Yang, Y.; Xu, J.H.
Sequence analysis and heterologous expression of a new cytochrome P450 monooxygenase from Rhodococcus sp. for asymmetric sulfoxidation
Appl. Microbiol. Biotechnol.
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Rhodococcus sp.
brenda
Pekthong, D.; Blanchard, N.; Abadie, C.; Bonet, A.; Heyd, B.; Mantion, G.; Berthelot, A.; Richert, L.; Martin, H.
Effects of Andrographis paniculata extract and Andrographolide on hepatic cytochrome P450 mRNA expression and monooxygenase activities after in vivo administration to rats and in vitro in rat and human hepatocyte cultures
Chem. Biol. Interact.
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Homo sapiens, Homo sapiens (P05177), Rattus norvegicus (P04799), Rattus norvegicus (P04800), Rattus norvegicus (P05182), Rattus norvegicus (P08683)
brenda
Robin, A.; Roberts, G.A.; Kisch, J.; Sabbadin, F.; Grogan, G.; Bruce, N.; Turner, N.J.; Flitsch, S.L.
Engineering and improvement of the efficiency of a chimeric [P450cam-RhFRed reductase domain] enzyme
Chem. Commun. (Camb. )
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synthetic construct
brenda
Liu, Y.; Glatt, H.
Human cytochrome P450 2E1 and sulfotransferase 1A1 coexpressed in Chinese hamster V79 cells enhance spontaneous mutagenesis
Environ. Mol. Mutagen.
51
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2010
Homo sapiens
brenda
Wright, A.T.; Song, J.D.; Cravatt, B.F.
A suite of activity-based probes for human cytochrome P450 enzymes
J. Am. Chem. Soc.
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Homo sapiens
brenda
Chen, C.K.; Berry, R.E.; Shokhireva, T.K.; Murataliev, M.B.; Zhang, H.; Walker, F.A.
Scanning chimeragenesis: the approach used to change the substrate selectivity of fatty acid monooxygenase CYP102A1 to that of terpene omega-hydroxylase CYP4C7
J. Biol. Inorg. Chem.
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Priestia megaterium (P14779)
brenda
Tam, T.W.; Liu, R.; Arnason, J.T.; Krantis, A.; Staines, W.A.; Haddad, P.S.; Foster, B.C.
Actions of ethnobotanically selected Cree anti-diabetic plants on human cytochrome P450 isoforms and flavin-containing monooxygenase 3
J. Ethnopharmacol.
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Homo sapiens, Homo sapiens (P05177), Homo sapiens (P10632), Homo sapiens (P10635), Homo sapiens (P20813), Homo sapiens (P20815), Homo sapiens (P24462)
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Hardstone, M.C.; Leichter, C.A.; Scott, J.G.
Multiplicative interaction between the two major mechanisms of permethrin resistance, kdr and cytochrome P450-monooxygenase detoxification, in mosquitoes
J. Evol. Biol.
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Culex quinquefasciatus
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Acharya, P.; Engel, J.C.; Correia, M.A.
Hepatic CYP3A suppression by high concentrations of proteasomal inhibitors: a consequence of endoplasmic reticulum (ER) stress induction, activation of RNA-dependent protein kinase-like ER-bound eukaryotic initiation factor 2alpha (eIF2alpha)-kinase (PERK)
Mol. Pharmacol.
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Rattus norvegicus
brenda
Diczfalusy, U.; Miura, J.; Roh, H.K.; Mirghani, R.A.; Sayi, J.; Larsson, H.; Bodin, K.G.; Allqvist, A.; Jande, M.; Kim, J.W.; Aklillu, E.; Gustafsson, L.L.; Bertilsson, L.
4Beta-hydroxycholesterol is a new endogenous CYP3A marker: relationship to CYP3A5 genotype, quinine 3-hydroxylation and sex in Koreans, Swedes and Tanzanians
Pharmacogenet. Genomics
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201-208
2008
Homo sapiens (P20815), Homo sapiens
brenda
Page, V.; Schwitzguebel, J.P.
Metabolism of sulphonated anthraquinones in rhubarb, maize and celery: the role of cytochromes P450 and peroxidases
Plant Cell Rep.
28
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Apium graveolens, Zea mays, Rheum rhaponticum
brenda
Pan, Y.; Michael, T.P.; Hudson, M.E.; Kay, S.A.; Chory, J.; Schuler, M.A.
Cytochrome P450 monooxygenases as reporters for circadian-regulated pathways
Plant Physiol.
150
858-878
2009
Arabidopsis thaliana
brenda
Furuya, T.; Shibata, D.; Kino, K.
Phylogenetic analysis of Bacillus P450 monooxygenases and evaluation of their activity towards steroids
Steroids
74
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2009
Bacillus cereus, Bacillus cereus (Q735A2), Bacillus cereus (Q735B3), Bacillus cereus (Q737F3), Bacillus cereus (Q737I9), Bacillus cereus (Q737J4)
brenda
Leoni, C.; Buratti, F.M.; Testai, E.
The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion
Toxicol. Appl. Pharmacol.
233
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2008
Homo sapiens, Homo sapiens (P05177), Homo sapiens (P10632), Homo sapiens (P10635), Homo sapiens (P11509), Homo sapiens (P20813)
brenda
Zhang, X.; Moore, J.N.; Newsted, J.L.; Hecker, M.; Zwiernik, M.J.; Jones, P.D.; Bursian, S.J.; Giesy, J.P.
Sequencing and characterization of mixed function monooxygenase genes CYP1A1 and CYP1A2 of Mink (Mustela vison) to facilitate study of dioxin-like compounds
Toxicol. Appl. Pharmacol.
234
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2009
Neogale vison (A7UDB5), Neogale vison (A7UDB6)
brenda
Beedanagari, S.R.; Bebenek, I.; Bui, P.; Hankinson, O.
Resveratrol inhibits dioxin-induced expression of human CYP1A1 and CYP1B1 by inhibiting recruitment of the aryl hydrocarbon receptor complex and RNA polymerase II to the regulatory regions of the corresponding genes
Toxicol. Sci.
110
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Homo sapiens
brenda
Nayeem, M.A.; Zeldin, D.C.; Boegehold, M.A.; Morisseau, C.; Marowsky, A.; Ponnoth, D.S.; Roush, K.P.; Falck, J.R.
Modulation by salt intake of the vascular response mediated through adenosine A(2A) receptor: role of CYP epoxygenase and soluble epoxide hydrolase
Am. J. Physiol. Regul. Integr. Comp. Physiol.
299
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Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Lamb, D.C.; Lei, L.; Zhao, B.; Yuan, H.; Jackson, C.J.; Warrilow, A.G.; Skaug, T.; Dyson, P.J.; Dawson, E.S.; Kelly, S.L.; Hachey, D.L.; Waterman, M.R.
Streptomyces coelicolor A3(2) CYP102 protein, a novel fatty acid hydroxylase encoded as a heme domain without an N-terminal redox partner
Appl. Environ. Microbiol.
76
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2010
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Flueck, C.E.; Mullis, P.E.; Pandey, A.V.
Reduction in hepatic drug metabolizing CYP3A4 activities caused by P450 oxidoreductase mutations identified in patients with disordered steroid metabolism
Biochem. Biophys. Res. Commun.
401
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2010
Homo sapiens
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Zhang, J.; Li, A.; Xu, J.
Improved expression of recombinant cytochrome P450 monooxygenase in Escherichia coli for asymmetric oxidation of sulfides
Bioprocess Biosyst. Eng.
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Rhodococcus sp.
brenda
Liu, L.; Schmid, R.D.; Urlacher, V.B.
Engineering cytochrome P450 monooxygenase CYP 116B3 for high dealkylation activity
Biotechnol. Lett.
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Rhodococcus ruber
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Brignac-Huber, L.; Reed, J.R.; Backes, W.L.
Organization of NADPH-cytochrome P450 reductase and CYP1A2 in the endoplasmic reticulum - microdomain localization affects monooxygenase function
Mol. Pharmacol.
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2011
Oryctolagus cuniculus
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Platt, K.L.; Edenharder, R.; Aderhold, S.; Muckel, E.; Glatt, H.
Fruits and vegetables protect against the genotoxicity of heterocyclic aromatic amines activated by human xenobiotic-metabolizing enzymes expressed in immortal mammalian cells
Mutat. Res.
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2010
Homo sapiens
brenda
Kobayashi, K.; Yamamoto, T.; Taguchi, M.; Chiba, K.
High-performance liquid chromatography determination of N- and O-demethylase activities of chemicals in human liver microsomes: application of postcolumn fluorescence derivatization using Nash reagent
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Homo sapiens, Rattus norvegicus
brenda
Syed, K.; Porollo, A.; Lam, Y.W.; Grimmett, P.E.; Yadav, J.S.
CYP63A2, a catalytically versatile fungal P450 monooxygenase capable of oxidizing higher-molecular-weight polycyclic aromatic hydrocarbons, alkylphenols, and alkanes
Appl. Environ. Microbiol.
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Phanerodontia chrysosporium
brenda
Schallmey, A.; Den Besten, G.; Teune, I.; Kembaren, R.; Janssen, D.
Characterization of cytochrome P450 monooxygenase CYP154H1 from the thermophilic soil bacterium Thermobifida fusca
Appl. Microbiol. Biotechnol.
89
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2011
Thermobifida fusca
brenda
Wang, S.P.; He, G.L.; Chen, R.R.; Li, F.; Li, G.Q.
The involvement of cytochrome P450 monooxygenases in methanol elimination in Drosophila melanogaster larvae
Arch. Insect Biochem. Physiol.
79
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2012
Drosophila melanogaster
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Ide, M.; Ichinose, H.; Wariishi, H.
Molecular identification and functional characterization of cytochrome P450 monooxygenases from the brown-rot basidiomycete Postia placenta
Arch. Microbiol.
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Postia placenta, Postia placenta MAD-698
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Misra, A.; Chanotiya, C.S.; Gupta, M.M.; Dwivedi, U.N.; Shasany, A.K.
Characterization of cytochrome P450 monooxygenases isolated from trichome enriched fraction of Artemisia annua L. leaf
Gene
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193-201
2012
Artemisia annua (Q2EPZ0), Artemisia annua
brenda
Lah, L.; Podobnik, B.; Novak, M.; Korosec, B.; Berne, S.; Vogelsang, M.; Krasevec, N.; Zupanec, N.; Stojan, J.; Bohlmann, J.; Komel, R.
The versatility of the fungal cytochrome P450 monooxygenase system is instrumental in xenobiotic detoxification
Mol. Microbiol.
81
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2011
Curvularia lunata
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Syed, K.; Porollo, A.; Miller, D.; Yadav, J.
Rational engineering of the fungal P450 monooxygenase CYP5136A3 to improve its oxidizing activity toward polycyclic aromatic hydrocarbons
Protein Eng.
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2013
Phanerodontia chrysosporium
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Roiban, G.; Agudo, R.; Ilie, A.; Lonsdale, R.; Reetz, M.
CH-activating oxidative hydroxylation of 1-tetralones and related compounds with high regio- and stereoselectivity
Chem. Commun. (Camb.)
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2014
Priestia megaterium (P14779), Priestia megaterium ATCC 14581 (P14779)
brenda
Kolrep, F.; Hessel, S.; These, A.; Ehlers, A.; Rein, K.; Lampen, A.
Differences in metabolism of the marine biotoxin okadaic acid by human and rat cytochrome P450 monooxygenases
Arch. Toxicol.
90
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2016
Homo sapiens, Rattus norvegicus (P04799), Rattus norvegicus (P04800)
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Matowane, R.; Wieteska, L.; Bamal, H.; Kgosiemang, I.; Van Wyk, M.; Manume, N.; Abdalla, S.; Mashele, S.; Gront, D.; Syed, K.
In silico analysis of cytochrome P450 monooxygenases in chrgranulomatous infectious fungus onic Sporothrix schenckii Special focus on CYP51
Biochim. Biophys. Acta
1866
166-177
2018
Sporothrix schenckii (U7Q7I7), Sporothrix schenckii, Sporothrix schenckii ATCC 58251 (U7Q7I7)
brenda
Yin, Y.; Yu, H.; Luan, Z.; Li, R.; Ouyang, P.; Liu, J.; Xu, J.
Unusually broad substrate profile of self-sufficient Cytochrome P450 monooxygenase CYP116B4 from Labrenzia aggregata
ChemBioChem
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2443-2449
2014
Roseibium aggregatum (A0P0F6), Roseibium aggregatum DSM 13394 (A0P0F6)
brenda
Wriessnegger, T.; Moser, S.; Emmerstorfer-Augustin, A.; Leitner, E.; Mueller, M.; Kaluzna, I.; Schuermann, M.; Mink, D.; Pichler, H.
Enhancing cytochrome P450-mediated conversions in P. pastoris through RAD52 over-expression and optimizing the cultivation conditions
Fungal Genet. Biol.
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2016
Homo sapiens (P10635), Homo sapiens
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Lee, H.; Kim, B.; Ahn, J.
Production of bioactive hydroxyflavones by using monooxygenase from Saccharothrix espanaensis
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Saccharothrix espanaensis (Q2EYY8)
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Tosstorff, A.; Dennig, A.; Ruff, A.; Schwaneberg, U.; Sieber, V.; Mangold, K.; Schrader, J.; Holtmann, D.
Mediated electron transfer with monooxygenases - Insight in interactions between reduced mediators and the co-substrate oxygen
J. Mol. Catal. B
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Priestia megaterium (P14779), Priestia megaterium DSM 32 (P14779)
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Hasegawa, E.; Inafuku, S.; Mulki, L.; Okunuki, Y.; Yanai, R.; Smith, K.; Kim, C.; Klokman, G.; Bielenberg, D.; Puli, N.; Falck, J.; Husain, D.; Miller, J.; Edin, M.; Zeldin, D.; Lee, K.; Hammock, B.; Schunck, W.; Connor, K.
Cytochrome P450 monooxygenase lipid metabolites are significant second messengers in the resolution of choroidal neovascularization
Proc. Natl. Acad. Sci. USA
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2017
Homo sapiens
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Lavado, R.; Li, J.; Rimoldi, J.; Schlenk, D.
Evaluation of the stereoselective biotransformation of permethrin in human liver microsomes Contributions of cytochrome P450 monooxygenases to the formation of estrogenic metabolites
Toxicol. Lett.
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2014
Homo sapiens
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Lau, I.; Feyereisen, R.; Nelson, D.; Bell, S.
Analysis and preliminary characterisation of the cytochrome P450 monooxygenases from Frankia sp. EuI1c (Frankia inefficax sp.)
Arch. Biochem. Biophys.
669
11-21
2019
Frankia inefficax (E3J2L4), Frankia inefficax (E3J531), Frankia inefficax (E3J9F8), Frankia inefficax DSM 45817 (E3J2L4), Frankia inefficax DSM 45817 (E3J531), Frankia inefficax DSM 45817 (E3J9F8)
brenda
Connick, J.P.; Reed, J.R.; Cawley, C.F.; Backes, W.L.
Heteromeric complex formation between human cytochrome P450 CYP1A1 and heme oxygenase-1
Biochem. J.
478
377-388
2021
Homo sapiens (P04798), Homo sapiens
brenda
Valikhani, D.; Bolivar, J.; Dennig, A.; Nidetzky, B.
A tailor-made, self-sufficient and recyclable monooxygenase catalyst based on coimmobilized cytochrome P450 BM3 and glucose dehydrogenase
Biotechnol. Bioeng.
115
2416-2425
2018
Priestia megaterium (P14779), Priestia megaterium DSM 32 (P14779)
-
brenda
Nair, P.C.; Gillani, T.B.; Rawling, T.; Murray, M.
Differential inhibition of human CYP2C8 and molecular docking interactions elicited by sorafenib and its major N-oxide metabolite
Chem. Biol. Interact.
338
109401
2021
Homo sapiens (P10632), Homo sapiens (P11712), Homo sapiens
brenda
Tang, L.W.T.; Teng, J.W.; Koh, S.K.; Zhou, L.; Go, M.L.; Chan, E.C.Y.
Mechanism-based inactivation of cytochrome P450 3A4 and 3A5 by the fibroblast growth factor receptor inhibitor erdafitinib
Chem. Res. Toxicol.
34
1800-1813
2021
Homo sapiens (P20815), Homo sapiens (Q9HB55)
brenda
Mukherjee, G.; Nandekar, P.P.; Wade, R.C.
An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase
Commun. Biol.
4
55
2021
Homo sapiens (P04798)
brenda
Indra, R.; Pompach, P.; Vavrova, K.; Jaklova, K.; Heger, Z.; Adam, V.; Eckschlager, T.; Kopeckova, K.; Arlt, V.A.; Stiborova, M.
Cytochrome P450 and flavin-containing monooxygenase enzymes are responsible for differential oxidation of the anti-thyroid-cancer drug vandetanib by human and rat hepatic microsomal systems
Environ. Toxicol. Pharmacol.
74
103310
2020
Rattus norvegicus (P08683)
brenda
Zhang, L.; Xie, Z.; Liu, Z.; Zhou, S.; Ma, L.; Liu, W.; Huang, J.; Ko, T.; Li, X.; Hu, Y.; Min, J.; Yu, X.; Guo, R.; Chen, C.
Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase
Nat. Commun.
11
2676
2020
Tepidiphilus thermophilus (A0A0K6ITW2)
brenda