Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.14.1 - unspecific monooxygenase and Organism(s) Homo sapiens and UniProt Accession P10635

for references in articles please use BRENDA:EC1.14.14.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A group of P-450 heme-thiolate proteins, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. Together with EC 1.6.2.4, NADPH---hemoprotein reductase, it forms a system in which two reducing equivalents are supplied by NADPH. Some of the reactions attributed to EC 1.14.15.3, alkane 1-monooxygenase, belong here.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P10635
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
p450, cyp2d6, cyp1a1, cyp2e1, cyp1a2, cyp2c9, cyp1b1, cyp3a5, cyp2b6, cyp1a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytochrome P450 monooxygenase
-
monooxygenase 3
-
3AH15
-
-
-
-
6 beta-hydroxylase
-
-
-
-
6-beta-testosterone hydroxylase
-
-
-
-
AA omega-hydroxylase
-
-
Aldehyde oxygenase
-
-
-
-
Arachidonic acid epoxygenase
-
-
-
-
aromatase
aryl hydrocarbon hydroxylase
-
-
-
-
aryl-4-monooxygenase
-
-
-
-
Brain aromatase
-
-
-
-
Clone PF26
-
-
-
-
Clone PF3/46
-
-
-
-
Coumarin 7-hydroxylase
-
-
-
-
CYP monooxygenase
-
-
CYP19
-
-
CYP1A1
CYP1A2
CYP1A3
-
-
-
-
CYP1B1
-
-
CYP24A1
-
-
CYP27A1
-
-
CYP2A3
-
-
-
-
CYP2A6
CYP2B6
CYP2C19
-
-
CYP2C8
CYP2C9
CYP3A4
CYP3A5
CYP4
-
-
CYP4502F4
-
-
-
-
CYP4A
-
-
CYP4F
-
-
CYP5A1
-
-
CYP6B1V1/CYP6B1V2/ CYP6B1V3
-
-
-
-
CYP6B3V1/CYP6B3V2
-
-
-
-
CYP6B4V1/CYP6B4V2
-
-
-
-
CYP6B5V1
-
-
-
-
CYP8A1
-
-
CYPIA1
-
-
-
-
CYPIA2
-
-
-
-
CYPIA4
-
-
-
-
CYPIA5
-
-
-
-
CYPIB1
-
-
-
-
CYPIIA1
-
-
-
-
CYPIIA10
-
-
-
-
CYPIIA11
-
-
-
-
CYPIIA12
-
-
-
-
CYPIIA13
-
-
-
-
CYPIIA2
-
-
-
-
CYPIIA3
-
-
-
-
CYPIIA4
-
-
-
-
CYPIIA5
-
-
-
-
CYPIIA6
-
-
-
-
CYPIIA7
-
-
-
-
CYPIIA8
-
-
-
-
CYPIIA9
-
-
-
-
CYPIIB1
-
-
-
-
CYPIIB10
-
-
-
-
CYPIIB11
-
-
-
-
CYPIIB12
-
-
-
-
CYPIIB19
-
-
-
-
CYPIIB2
-
-
-
-
CYPIIB20
-
-
-
-
CYPIIB3
-
-
-
-
CYPIIB4
-
-
-
-
CYPIIB5
-
-
-
-
CYPIIB6
-
-
-
-
CYPIIB9
-
-
-
-
CYPIIC1
-
-
-
-
CYPIIC10
-
-
-
-
CYPIIC11
-
-
-
-
CYPIIC12
-
-
-
-
CYPIIC13
-
-
-
-
CYPIIC14
-
-
-
-
CYPIIC15
-
-
-
-
CYPIIC16
-
-
-
-
CYPIIC17
-
-
-
-
CYPIIC18
-
-
-
-
CYPIIC19
-
-
-
-
CYPIIC2
-
-
-
-
CYPIIC20
-
-
-
-
CYPIIC21
-
-
-
-
CYPIIC22
-
-
-
-
CYPIIC23
-
-
-
-
CYPIIC24
-
-
-
-
CYPIIC25
-
-
-
-
CYPIIC26
-
-
-
-
CYPIIC27
-
-
-
-
CYPIIC28
-
-
-
-
CYPIIC29
-
-
-
-
CYPIIC3
-
-
-
-
CYPIIC30
-
-
-
-
CYPIIC31
-
-
-
-
CYPIIC37
-
-
-
-
CYPIIC38
-
-
-
-
CYPIIC39
-
-
-
-
CYPIIC4
-
-
-
-
CYPIIC40
-
-
-
-
CYPIIC41
-
-
-
-
CYPIIC42
-
-
-
-
CYPIIC5
-
-
-
-
CYPIIC6
-
-
-
-
CYPIIC7
-
-
-
-
CYPIIC8
-
-
-
-
CYPIIC9
-
-
-
-
CYPIID1
-
-
-
-
CYPIID10
-
-
-
-
CYPIID11
-
-
-
-
CYPIID14
-
-
-
-
CYPIID15
-
-
-
-
CYPIID16
-
-
-
-
CYPIID17
-
-
-
-
CYPIID18
-
-
-
-
CYPIID19
-
-
-
-
CYPIID2
-
-
-
-
CYPIID3
-
-
-
-
CYPIID4
-
-
-
-
CYPIID5
-
-
-
-
CYPIID6
-
-
-
-
CYPIID9
-
-
-
-
CYPIIE1
-
-
-
-
CYPIIF1
-
-
-
-
CYPIIF3
-
-
-
-
CYPIIF4
-
-
-
-
CYPIIG1
-
-
-
-
CYPIIH1
-
-
-
-
CYPIIH2
-
-
-
-
CYPIIIA1
-
-
-
-
CYPIIIA10
-
-
-
-
CYPIIIA11
-
-
-
-
CYPIIIA12
-
-
-
-
CYPIIIA13
-
-
-
-
CYPIIIA14
-
-
-
-
CYPIIIA15
-
-
-
-
CYPIIIA16
-
-
-
-
CYPIIIA17
-
-
-
-
CYPIIIA18
-
-
-
-
CYPIIIA19
-
-
-
-
CYPIIIA2
-
-
-
-
CYPIIIA21
-
-
-
-
CYPIIIA24
-
-
-
-
CYPIIIA25
-
-
-
-
CYPIIIA27
-
-
-
-
CYPIIIA28
-
-
-
-
CYPIIIA29
-
-
-
-
CYPIIIA3
-
-
-
-
CYPIIIA30
-
-
-
-
CYPIIIA31
-
-
-
-
CYPIIIA5
-
-
-
-
CYPIIIA6
-
-
-
-
CYPIIIA7
-
-
-
-
CYPIIIA8
-
-
-
-
CYPIIIA9
-
-
-
-
CYPIIJ1
-
-
-
-
CYPIIJ2
-
-
-
-
CYPIIJ3
-
-
-
-
CYPIIJ5
-
-
-
-
CYPIIJ6
-
-
-
-
CYPIIK1
-
-
-
-
CYPIIK3
-
-
-
-
CYPIIK4
-
-
-
-
CYPIIL1
-
-
-
-
CYPIIM1
-
-
-
-
CYPIVA4
-
-
-
-
CYPIVA8
-
-
-
-
CYPIVB1
-
-
-
-
CYPIVC1
-
-
-
-
CYPIVF1
-
-
-
-
CYPIVF11
-
-
-
-
CYPIVF12
-
-
-
-
CYPIVF4
-
-
-
-
CYPIVF5
-
-
-
-
CYPIVF6
-
-
-
-
CYPIVF8
-
-
-
-
CYPVIA1
-
-
-
-
CYPVIB1
-
-
-
-
CYPVIB2
-
-
-
-
CYPVIB4
-
-
-
-
CYPVIB5
-
-
-
-
CYPVIB6
-
-
-
-
CYPVIB7
-
-
-
-
CYPXIX
-
-
-
-
CYPXIXA1
-
-
-
-
CYPXIXA2
-
-
-
-
CYPXIXA3
-
-
-
-
cytochrome P-450 4 enzyme
-
-
cytochrome P450 3A4
-
-
cytochrome P450 monooxygenase
cytochrome P450 monooxygenase 2A6
-
-
cytochrome P450 monooxygenase 2C8
-
-
cytochrome P450 monooxygenase 2C9
-
-
cytochrome P450 monooxygenase 3A4
-
-
cytochrome P450 oxidoreductase
-
-
Cytochrome P450-D2
-
-
-
-
cytochrome P450-dependent monooxygenase 1A2
-
-
DAH1
-
-
-
-
DAH2
-
-
-
-
Debrisoquine 4-hydroxylase
-
-
-
-
Estrogen synthetase
-
-
-
-
flavoprotein monooxygenase
-
-
-
-
flavoprotein-linked monooxygenase
-
-
-
-
Hepatic cytochrome P-450MC1
-
-
-
-
HLp
-
-
-
-
IIA3
-
-
-
-
Isozyme 3A
-
-
-
-
Laurate omega-1 hydroxylase
-
-
-
-
Lauric acid omega-6-hydroxylase
-
-
-
-
LMC1
-
-
-
-
Mephenytoin 4-hydroxylase
-
-
-
-
microsomal monooxygenase
-
-
-
-
microsomal P-450
-
-
-
-
N-demethylase
-
-
nicotine oxidase
-
CYP2A6
O-demethylase
-
-
OLF2
-
-
-
-
Olfactive
-
-
-
-
Ovarian aromatase
-
-
-
-
oxygenase, flavoprotein-linked mono-
-
-
-
-
P(3)450
-
-
-
-
P-448
-
-
-
-
P-450 PHPAH1
-
-
-
-
P-450(M-1)
-
-
-
-
P-450-MK2
-
-
-
-
P-450AROM
-
-
-
-
P-450IB
-
-
-
-
P-450IIIAM1
-
-
-
-
P-450MC
-
-
-
-
P-450MP
-
-
-
-
P-450UT
-
-
-
-
P1-88
-
-
-
-
P24
-
-
-
-
P450
-
-
P450 17-alpha
-
-
-
-
P450 19A1
-
-
P450 1A1
-
-
P450 1A2
-
-
P450 1B1
-
-
P450 2A6
-
-
P450 2B6
-
-
P450 2C19
-
-
P450 2C9
-
-
P450 2D-29/2D-35
-
-
-
-
P450 2D6
-
-
P450 2E1
-
-
P450 2J2
-
-
P450 3A4
-
-
P450 4A11
-
-
P450 4F2
-
-
P450 CM3A-10
-
-
-
-
P450 DUT2
-
-
-
-
P450 FA
-
-
-
-
P450 FI
-
-
-
-
P450 form 3B
-
-
-
-
P450 form HP1
-
-
-
-
P450 HSM1
-
-
-
-
P450 HSM2
-
-
-
-
P450 HSM3
-
-
-
-
P450 HSM4
-
-
-
-
P450 IIB1
-
-
-
-
P450 IIC2
-
-
-
-
P450 LM4
-
-
-
-
P450 LM6
-
-
-
-
P450 LMC2
-
-
-
-
P450 MD
-
-
-
-
P450 MP-12/MP-20
-
-
-
-
P450 P49
-
-
-
-
P450 PB1
-
-
-
-
P450 PB4
-
-
-
-
P450 PBC1
-
-
-
-
P450 PBC2
-
-
-
-
P450 PBC3
-
-
-
-
P450 PBC4
-
-
-
-
P450 PCHP3
-
-
-
-
P450 PCHP7
-
-
-
-
P450 TCDDAA
-
-
-
-
P450 TCDDAHH
-
-
-
-
P450 type B2
-
-
-
-
P450 types B0 and B1
-
-
-
-
P450(I)
-
-
-
-
P450-11A
-
-
-
-
P450-15-alpha
-
-
-
-
P450-15-COH
-
-
-
-
P450-16-alpha
-
-
-
-
P450-254C
-
-
-
-
P450-3C
-
-
-
-
P450-6B/29C
-
-
-
-
P450-A3
-
-
-
-
P450-AFB
-
-
-
-
P450-ALC
-
-
-
-
P450-CMF1A
-
-
-
-
P450-CMF1B
-
-
-
-
P450-CMF2
-
-
-
-
P450-CMF3
-
-
-
-
P450-DB1
-
-
-
-
P450-DB2
-
-
-
-
P450-DB3
-
-
-
-
P450-DB4
-
-
-
-
P450-DB5
-
-
-
-
P450-HFLA
-
-
-
-
P450-HP
-
-
-
-
P450-IIA10
-
-
-
-
P450-IIA11
-
-
-
-
P450-IIA3.1
-
-
-
-
P450-IIA3.2
-
-
-
-
P450-IIA4
-
-
-
-
P450-KP1
-
-
-
-
P450-LM2
-
-
-
-
P450-MC1
-
-
-
-
P450-MC4
-
-
-
-
P450-MK1
-
-
-
-
P450-MKJ1
-
-
-
-
P450-MKMP13
-
-
-
-
P450-MKNF2
-
-
-
-
P450-NMB
-
-
-
-
P450-OLF1
-
-
-
-
P450-OLF3
-
-
-
-
P450-P1
-
-
-
-
P450-P2/P450-P3
-
-
-
-
P450-P3
-
-
-
-
P450-PB1 and P450-PB2
-
-
-
-
P450-PCN1
-
-
-
-
P450-PCN2
-
-
-
-
P450-PCN3
-
-
-
-
P450-PM4
-
-
-
-
P450-PP1
-
-
-
-
P450-PROS2
-
-
-
-
P4501A1
-
-
-
-
P450CB
-
-
-
-
P450CMEF
-
-
-
-
P450E
-
-
-
-
P450EF
-
-
-
-
P450F
-
-
-
-
P450H
-
-
-
-
P450I
-
-
-
-
P450IIC5
-
-
-
-
P450MT2
-
-
-
-
P450RAP
-
-
-
-
P450RLM6
-
-
-
-
P52
-
-
-
-
PB15
-
-
-
-
PHP2
-
-
-
-
PHP3
-
-
-
-
Progesterone 21-hydroxylase
-
-
-
-
Prostaglandin omega-hydroxylase
-
-
-
-
PTF1
-
-
-
-
PTF2
-
-
-
-
S-mephenytoin 4-hydroxylase
-
-
-
-
sertraline N-demethylase
-
-
Steroid hormones 7-alpha-hydroxylase
-
-
-
-
Testosterone 15-alpha-hydroxylase
-
-
-
-
Testosterone 16-alpha hydroxylase
-
-
-
-
Testosterone 6-beta-hydroxylase
-
-
-
-
Testosterone 7-alpha-hydroxylase
-
-
-
-
xenobiotic monooxygenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
sulfoxidation
-
-
-
-
hydroxylation
-
-
-
-
epoxidation
-
-
-
-
N-oxidation
-
-
-
-
O-dealkylation
-
-
-
-
desulfation
-
-
-
-
reduction of azo, nitro, N-oxide groups
-
-
-
-
N-dealkylation
-
-
-
-
S-dealkylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
substrate,NADPH-hemoprotein reductase:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)
A group of P-450 heme-thiolate proteins, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. Together with EC 1.6.2.4, NADPH---hemoprotein reductase, it forms a system in which two reducing equivalents are supplied by NADPH. Some of the reactions attributed to EC 1.14.15.3, alkane 1-monooxygenase, belong here.
CAS REGISTRY NUMBER
COMMENTARY hide
62213-32-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-[2-(N,N-diethyl-N-methylammonium)ethyl]-7-methoxy-4-methylcoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
fenthion + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
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
-
-
?
(1R)-cis-permethrin + O2 + [reduced NADPH-hemoprotein reductase]
3-phenoxybenzyl alcohol + 3-(4'-hydroxyphenoxy)-benzyl alcohol + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
-
-
-
-
?
(1R)-trans-permethrin + O2 + [reduced NADPH-hemoprotein reductase]
3-phenoxybenzyl alcohol + 3-(4'-hydroxyphenoxy)-benzyl alcohol + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
-
-
-
-
?
(1S)-cis-permethrin + O2 + [reduced NADPH-hemoprotein reductase]
3-phenoxybenzyl alcohol + 3-(4'-hydroxyphenoxy)-benzyl alcohol + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
-
-
-
-
?
(1S)-trans-permethrin + O2 + [reduced NADPH-hemoprotein reductase]
3-phenoxybenzyl alcohol + 3-(4'-hydroxyphenoxy)-benzyl alcohol + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
-
-
-
-
?
(S)-nicotine + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
substrate of CYP3A4, the reaction involves electron transfer via FMN
-
-
?
2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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.
-
-
?
3-cyano-7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
4-(methylnitrosamino)-1-(3pyridyl)-1-butanone + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
show the reaction diagram
-
wild-type enzyme and recombinant enzyme P4502B6 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
resorufin + ethanol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
7-methoxy-4-(trifluoromethyl)-coumarin + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
7-methoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
-
?
adrenic acid + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
i.e. all-cis-7,10,13,16-docosatetraenoic acid
-
-
?
aminopyrine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
amiprofos-methyl + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
show the reaction diagram
-
-
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
?
show the reaction diagram
-
-
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
recombinant wild-type enzyme and enzyme mutant fused to yeast reductase expressed in transgenic potato plants
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
chlorzoxazone + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
-
?
dibenzylfluorescein + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
dimethylaniline + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
substrate of CYP3A4
-
-
?
docosahexaenoic acid + [reduced NADPH-hemoprotein reductase] + O2
22-hydroxydocosahexaenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
eicosapentaenoic acid + NADPH + H+ + O2
20-hydroxyeicosapentaenoic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
erythromycin + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
fenthion + NADPH + H+ + O2
fenthion-oxon + sulfur + NADP+ + H2O
show the reaction diagram
-
-
-
r
fenthion + NADPH + H+ + O2
fenthion-sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
r
fenthion + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
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
show the reaction diagram
fluoxetine + [reduced NADPH-hemoprotein reductase] + O2
? + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
(9Z,12Z)-18-hydroxyoctadeca-9,12-dienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
losartan + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
mefenacet + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
midazolam + [reduced NADPH-hemoprotein reductase] + O2
1'-hydroxymidazolam + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
N'-nitrosonornicotine + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
norflurazon + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
okadaic acid + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
p-nitrophenol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
CYP2E1
-
-
?
paclitaxel + [reduced NADPH-hemoprotein reductase] + O2
6alpha-hydroxypaclitaxel + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
pendimethalin + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
pyributicarb + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
quinine + [reduced NADPH-hemoprotein reductase] + O2
3-hydroxyquinine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
rivaroxaban + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
S-mephenytoin + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
-
?
sertraline + [reduced NADPH-hemoprotein reductase] + O2
demethylsertraline + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
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
show the reaction diagram
testosterone + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
CYP3A4
-
-
?
tolbutamide + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
CYP2C9
-
-
?
trifluralin + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-(methylnitrosamino)-1-(3pyridyl)-1-butanone + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
wild-type enzyme and recombinant enzyme P4502B6 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
show the reaction diagram
-
-
i.e. 20-HETE, a potent constrictor of renal microvessels and inhibits Na+ reabsorption in the proximal tubule and thick ascending limb
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
recombinant wild-type enzyme and enzyme mutant fused to yeast reductase expressed in transgenic potato plants
-
-
?
N'-nitrosonornicotine + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
nicotine oxidase activity of CYP2A6, activates the tobacco-derived carcinogens to mutagenic products
-
-
?
quinine + [reduced NADPH-hemoprotein reductase] + O2
3-hydroxyquinine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
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
-
-
?
sertraline + [reduced NADPH-hemoprotein reductase] + O2
demethylsertraline + formaldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
i.e. (1S,4S)-N-methyl-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydro-1-naphthylamine, a one-step oxidative N-demethylation
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
a heme-thiolate protein (P-450)
-
NADPH
cytochrome P450
-
-
-
flavoprotein
-
-
-
heme
-
the heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions
NADH
-
-
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methanol
partially affects (10-20%) activity of the active recombinant enzyme
1-aminobenzotriazole
-
moderately prohibits spontaneous mutations of V79-hCYP2E1-hSULT1A1 cells. In combination with SULT1A1 inhibitor pentachlorophenol completely prohibits spontaneous mutations of V79-hCYP2E1-hSULT1A1 cells
17alpha-ethynylestradiol
-
reactive intermediates of 17alpha-ethynylestradiol inactivate P450s in a NADPH-dependent mechanism-based manner by a combination of heme alkylation and apoprotein modification
8-methoxypsoralen
-
-
anastrozole
-
profiling inhibition of probe 1 labeling of P450 19A1, inhibits labeling of P450 2C9 by probe 5
cimetidine
-
specific inhibition
diethyldithiocarbamate
CYP2E1
Emulgen
-
a detergent that inactivates the enzyme at high concentrations
-
erdafitinib
fibroblast growth factor receptor inhibitor, irreversible covalent mechanism-based inhibitor of both isoforms CYP3A4 and CYP3A5
-
formestane
-
profiling inhibition of probe 1 labeling of P450 19A1, decreases probe 5 labeling of P450 2C19 and 1 labeling of P450 3A4
furafylline
ketoconazole
methanol
sorafenib N-oxide
-
sulfaphenazole
ticlopidine
CYP2B6 and CYP2C19, 40% loss of sulfoxide formation. Decrease in fenthion-oxon formation by 71% and 64% at 0.005 mM or 0.1 mM fenthion concentrations, respectively, which is mainly attributable to CYP2B6
tranylcypromine
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
anastrozole
-
increases labeling of P450 1A2 by probe 3 up to 175% of control values
NADPH-P450 reductase
-
supports the CYP3A4 activity through providing NADPH, mutations in NADPH-P450 reductase, identified in patients with disordered steroidogenesis/Antley-Bixler syndrome, reduce CYP3A4 activity. NADPH-P450 reductase mutants Y181D, A457H, Y459H, V492E and R616X loose more than 99% of CYP3A4 activity, while NADPH-P450 reductase mutations A287P, C569Y and V608F loose 60-85% activity
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.055 - 0.061
(1R)-cis-permethrin
0.115 - 0.131
(1R)-trans-permethrin
0.057 - 0.063
(1S)-cis-permethrin
0.101 - 0.106
(1S)-trans-permethrin
0.0001 - 0.0012
7-ethoxyresorufin
0.0016 - 0.131
fenthion
0.018
fenthion-sulfoxide
CYP2C19
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 0.01
erdafitinib
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
anastrozole
Homo sapiens
-
P450 19A1
0.00043
formestane
Homo sapiens
-
P450 19A1
0.036 - 0.051
sorafenib
0.014 - 0.04
sorafenib N-oxide
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
CYP1A1 and CYP1A2
Manually annotated by BRENDA team
-
CYP1A1, CYP1A2 and CYP1B1
Manually annotated by BRENDA team
additional information
-
isozyme tissue-specific expression analysis, regulation by PPAR
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
CYP24A1 and CYP27A1
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
-
loss of CYP3A4 activity may result in increased risk of drug toxicities and adverse drug reactions in patients with NADPH-P450 reductase mutations
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CP2D6_HUMAN
497
0
55769
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
x * 52000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
genetic variations, substantial effects of single nucleotide polymorphisms, e.g. CYP2D6 and CYP2C19 SNPs show large e.ects on metabolism of debrisoquine and (S)-mephenytoin, respectively, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
in absence of NADPH, the enzyme retains about 85% of the CYP functional activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially by microsome preparation
-
recombinant enzyme from Escherichia coli by anion exchange chromatography and gel filtration to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
baculovirus-infected insect cells expressing single c-DNA-derived CYPs
microsomes derived from baculovirus infected insect cells expressing CYP2D6
overexpression in Pichia pastoris. RAD52 overexpression in Pichia pastoris CYP2D6-hCPR leads to twofold enhanced 1'-hydroxy bufuralol formation after cultivation and induction at pH 6, while shifting cultivation and induction to pH 8 is similarly effective. The beneficial effects are largely additive yielding in about 3fold more bufuralol hydroxylation in Pichia pastoris CYP2D6-hCPR-RAD52 than in the initial strain and condition
baculovirus-infected insect cells expressing single c-DNA-derived CYPs
coexpression of CYP1A2 with the Y459H and V492E mutant POR alleles in tBTC1A2_POR cell-models
-
expression analysis of human CYPS, overvuew, expression in Escherichia coli without the N-terminal leader sequence
-
expression in HepG2 cells
-
expression in V79 Chinese hamster fibroblasts and Hep-G2 cells, coexpression with N(O)-acetyltransferase or sulfotransferase 1A1-1
-
expression of recombinant human P4502B6 and yeast reductase fused enzyme in transgenic tobacco plants, integration into the tobacco genome, functional expression of CYP1A1 and CYP1A1-yeast reductase fused enzyme in transgenic potato plants, genetic transformation is mediated by Agrobacterium tumefaciens
-
microsomes derived from baculovirus infected insect cells expressing CYP1A2
microsomes derived from baculovirus infected insect cells expressing CYP2B6
microsomes derived from baculovirus infected insect cells expressing CYP2C8
microsomes derived from baculovirus infected insect cells expressing CYP2C9, CYP2C19, CYP2E1, CYP3A4, or CYP19
microsomes derived from baculovirus infected insect cells expressing CYP3A5
microsomes derived from baculovirus infected insect cells expressing CYP3A7
recombinant cDNA P450s coexpressed with cytochrome P450 reductase in insect cell microsomes
-
recombinant expression in Escherichia coli
-
V79-hCYP2E1 (constructed by transfection of CYP2E1-expressing vector pSV together with vector pSV2neo containing a G418-selective marker into V79-Mz cells) and SULT1A1 expression vector introduced into this cell line
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
0.0001 mM dioxin treatment for 24, 48, and 72 h induces CYP1A1, CYP1A2 and CYP1B1 mRNA levels
-
beta-naphthoflavone (0.05 mM) causes a 9fold increase in CYP1A2-dependent activity and a 25fold increase in CYP1A2 mRNA expression in hepatocyte microsomes
dexamethasone (0.05 mM) and rifampicin (0.01 mM) increase CYP3A4 mRNA expression by a mean of 14fold in hepatocytes
in hepatocyte cultures, treatment with 0.05 mM Andrographis paniculata extract results in a slight decrease of CYP1A2 (30%) enzymatic activities
in hepatocyte cultures, treatment with 0.05 mM Andrographis paniculata extract results in a slight decrease of CYP2E1 (20%) enzymatic activities, whereas CYP2C9- and CYP3A4-dependent monooxygenase activities are significantly decreased by 40% and 60%, respectively. Andrographolide causes a 30% decrease in CYP2C9- and CYP3A4-dependent monooxygenase activities, which is not significant
mutations in NADPH-P450 reductase, identified in patients with disordered steroidogenesis/Antley-Bixler syndrome, reduce CYP3A4 activity. NADPH-P450 reductase mutants Y181D, A457H, Y459H, V492E and R616X loose more than 99% of CYP3A4 activity, while NADPH-P450 reductase mutations A287P, C569Y and V608F loose 60-85% activity
-
resveratrol inhibits dioxin-induced expression of CYP1A1, CYP1A2 and CYP1B1 by directly or indirectly inhibiting the recruitment of the transcription factors aryl hydrocarbon receptor and aryl hydrocarbon nuclear translocator to the xenobiotic response elements of the corresponding genes
-
V79-hCYP2E1-hSULT1A1 cells contain a higher level of hCYP2E1 protein than the parental V79-hCYP2E1 line (by a factor of 3–4)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
enzyme expressed in Oryza sativa results in high tolerance to herbicides mefenacet, pyributicarb, amiprofos-methyl, trifluralin, pendimethalin, norflurazon, chlorotoluron and five chloroacetamides
biotechnology
most Cree anti-diabetic plant ethanolic extracts have the potential to affect CYP2C- and 3A4-mediated metabolism, and have the potential to affect the bioavailability and pharmacokinetics of conventional and traditional medicines during concomitant use, thus there is a potential risk of interactions if these traditional medicines are used with conventional therapeutic products, but several extracts may also have the potential to pharmacoenhance the activity of some medicines
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Johnson, E.F.; Stout, C.D.
Structural diversity of human xenobiotic-metabolizing cytochrome P450 monooxygenases
Biochem. Biophys. Res. Commun.
338
331-336
2005
Homo sapiens
Manually annotated by BRENDA team
Cashman, J.R.
Some distinctions between flavin-containing and cytochrome P450 monooxygenases
Biochem. Biophys. Res. Commun.
338
599-604
2005
Homo sapiens
Manually annotated by BRENDA team
Gorinova, N.; Nedkovska, M.; Atanassov, A.
Cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants
Biotechnol. Biotechnol. Equip.
19
105-115
2005
Homo sapiens, Lolium rigidum, Nicotiana tabacum, Phelipanche ramosa, Rattus norvegicus, Solanum tuberosum, Sorghum sp., Triticum aestivum, Zea mays
-
Manually annotated by BRENDA team
Ito, O.; Nakamura, Y.; Tan, L.; Ishizuka, T.; Sasaki, Y.; Minami, N.; Kanazawa, M.; Ito, S.; Sasano, H.; Kohzuki, M.
Expression of cytochrome P-450 4 enzymes in the kidney and liver: regulation by PPAR and species-difference between rat and human
Mol. Cell. Biochem.
284
141-148
2006
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kranendonk, M.; Marohnic, C.C.; Panda, S.P.; Duarte, M.P.; Oliveira, J.S.; Masters, B.S.; Rueff, J.
Impairment of human CYP1A2-mediated xenobiotic metabolism by Antley-Bixler syndrome variants of cytochrome P450 oxidoreductase
Arch. Biochem. Biophys.
475
93-99
2008
Homo sapiens
Manually annotated by BRENDA team
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.
65
303-306
2008
Homo sapiens
Manually annotated by BRENDA team
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.
179
247-255
2009
Homo sapiens, Homo sapiens (P05177), Rattus norvegicus (P04799), Rattus norvegicus (P04800), Rattus norvegicus (P05182), Rattus norvegicus (P08683)
Manually annotated by BRENDA team
Liu, Y.; Glatt, H.
Human cytochrome P450 2E1 and sulfotransferase 1A1 coexpressed in Chinese hamster V79 cells enhance spontaneous mutagenesis
Environ. Mol. Mutagen.
51
23-30
2010
Homo sapiens
Manually annotated by BRENDA team
Wright, A.T.; Song, J.D.; Cravatt, B.F.
A suite of activity-based probes for human cytochrome P450 enzymes
J. Am. Chem. Soc.
131
10692-10700
2009
Homo sapiens
Manually annotated by BRENDA team
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.
126
119-126
2009
Homo sapiens, Homo sapiens (P05177), Homo sapiens (P10632), Homo sapiens (P10635), Homo sapiens (P20813), Homo sapiens (P20815), Homo sapiens (P24462)
Manually annotated by BRENDA team
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
18
201-208
2008
Homo sapiens (P20815), Homo sapiens
Manually annotated by BRENDA team
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
343-352
2008
Homo sapiens, Homo sapiens (P05177), Homo sapiens (P10632), Homo sapiens (P10635), Homo sapiens (P11509), Homo sapiens (P20813)
Manually annotated by BRENDA team
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
61-67
2009
Homo sapiens
Manually annotated by BRENDA team
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
R325-R333
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
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
149-153
2010
Homo sapiens
Manually annotated by BRENDA team
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.
703
90-98
2010
Homo sapiens
Manually annotated by BRENDA team
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
Anal. Biochem.
284
342-347
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
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
2025-2036
2016
Homo sapiens, Rattus norvegicus (P04799), Rattus norvegicus (P04800)
Manually annotated by BRENDA team
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.
89
114-125
2016
Homo sapiens (P10635), Homo sapiens
Manually annotated by BRENDA team
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
114
E7545-E7553
2017
Homo sapiens
Manually annotated by BRENDA team
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.
226
192-197
2014
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team