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Information on EC 1.14.14.1 - unspecific monooxygenase and Organism(s) Mus musculus

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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.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
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
-
-
-
-
CYP1A1
-
-
-
-
CYP1A2
-
-
-
-
CYP1A3
-
-
-
-
CYP2A3
-
-
-
-
CYP4502F4
-
-
-
-
CYP4F2
-
-
CYP4F3A
-
-
CYP4F3B
-
-
CYP6B1V1/CYP6B1V2/ CYP6B1V3
-
-
-
-
CYP6B3V1/CYP6B3V2
-
-
-
-
CYP6B4V1/CYP6B4V2
-
-
-
-
CYP6B5V1
-
-
-
-
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
-
-
-
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CYPIIC21
-
-
-
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CYPIIC22
-
-
-
-
CYPIIC23
-
-
-
-
CYPIIC24
-
-
-
-
CYPIIC25
-
-
-
-
CYPIIC26
-
-
-
-
CYPIIC27
-
-
-
-
CYPIIC28
-
-
-
-
CYPIIC29
-
-
-
-
CYPIIC3
-
-
-
-
CYPIIC30
-
-
-
-
CYPIIC31
-
-
-
-
CYPIIC37
-
-
-
-
CYPIIC38
-
-
-
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CYPIIC39
-
-
-
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CYPIIC4
-
-
-
-
CYPIIC40
-
-
-
-
CYPIIC41
-
-
-
-
CYPIIC42
-
-
-
-
CYPIIC5
-
-
-
-
CYPIIC6
-
-
-
-
CYPIIC7
-
-
-
-
CYPIIC8
-
-
-
-
CYPIIC9
-
-
-
-
CYPIID1
-
-
-
-
CYPIID10
-
-
-
-
CYPIID11
-
-
-
-
CYPIID14
-
-
-
-
CYPIID15
-
-
-
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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
-
-
-
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CYPIIIA19
-
-
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CYPIIIA2
-
-
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CYPIIIA21
-
-
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CYPIIIA24
-
-
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CYPIIIA25
-
-
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CYPIIIA27
-
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CYPIIIA28
-
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CYPIIIA29
-
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CYPIIIA3
-
-
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CYPIIIA30
-
-
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CYPIIIA31
-
-
-
-
CYPIIIA5
-
-
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CYPIIIA6
-
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CYPIIIA7
-
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CYPIIIA8
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CYPIIIA9
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CYPIIJ1
-
-
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CYPIIJ2
-
-
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CYPIIJ3
-
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CYPIIJ5
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CYPIIJ6
-
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CYPIIK1
-
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CYPIIK3
-
-
-
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CYPIIK4
-
-
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CYPIIL1
-
-
-
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CYPIIM1
-
-
-
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CYPIVA4
-
-
-
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CYPIVA8
-
-
-
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CYPIVB1
-
-
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CYPIVC1
-
-
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CYPIVF1
-
-
-
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CYPIVF11
-
-
-
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CYPIVF12
-
-
-
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CYPIVF4
-
-
-
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CYPIVF5
-
-
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CYPIVF6
-
-
-
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CYPIVF8
-
-
-
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CYPVIA1
-
-
-
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CYPVIB1
-
-
-
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CYPVIB2
-
-
-
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CYPVIB4
-
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CYPVIB5
-
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CYPVIB6
-
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CYPVIB7
-
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CYPXIX
-
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CYPXIXA1
-
-
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CYPXIXA2
-
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CYPXIXA3
-
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Cytochrome P450-D2
-
-
-
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DAH1
-
-
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DAH2
-
-
-
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Debrisoquine 4-hydroxylase
-
-
-
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Estrogen synthetase
-
-
-
-
flavoprotein monooxygenase
-
-
-
-
flavoprotein-linked monooxygenase
-
-
-
-
Hepatic cytochrome P-450MC1
-
-
-
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HLp
-
-
-
-
IIA3
-
-
-
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Isozyme 3A
-
-
-
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Laurate omega-1 hydroxylase
-
-
-
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Lauric acid omega-6-hydroxylase
-
-
-
-
LMC1
-
-
-
-
Mephenytoin 4-hydroxylase
-
-
-
-
microsomal monooxygenase
-
-
-
-
microsomal P-450
-
-
-
-
OLF2
-
-
-
-
Olfactive
-
-
-
-
Ovarian aromatase
-
-
-
-
oxygenase, flavoprotein-linked mono-
-
-
-
-
P(3)450
-
-
-
-
P-448
-
-
-
-
P-450 PHPAH1
-
-
-
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P-450(M-1)
-
-
-
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P-450-MK2
-
-
-
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P-450AROM
-
-
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P-450IB
-
-
-
-
P-450IIIAM1
-
-
-
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P-450MC
-
-
-
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P-450MP
-
-
-
-
P-450UT
-
-
-
-
P1-88
-
-
-
-
P24
-
-
-
-
P450 17-alpha
-
-
-
-
P450 2D-29/2D-35
-
-
-
-
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
-
-
-
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P450(I)
-
-
-
-
P450-11A
-
-
-
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P450-15-alpha
-
-
-
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P450-15-COH
-
-
-
-
P450-16-alpha
-
-
-
-
P450-254C
-
-
-
-
P450-3C
-
-
-
-
P450-6B/29C
-
-
-
-
P450-A3
-
-
-
-
P450-AFB
-
-
-
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P450-ALC
-
-
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P450-CMF1A
-
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P450-CMF1B
-
-
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P450-CMF2
-
-
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P450-CMF3
-
-
-
-
P450-DB1
-
-
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P450-DB2
-
-
-
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P450-DB3
-
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P450-DB4
-
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P450-DB5
-
-
-
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P450-HFLA
-
-
-
-
P450-HP
-
-
-
-
P450-IIA10
-
-
-
-
P450-IIA11
-
-
-
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P450-IIA3.1
-
-
-
-
P450-IIA3.2
-
-
-
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P450-IIA4
-
-
-
-
P450-KP1
-
-
-
-
P450-LM2
-
-
-
-
P450-MC1
-
-
-
-
P450-MC4
-
-
-
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P450-MK1
-
-
-
-
P450-MKJ1
-
-
-
-
P450-MKMP13
-
-
-
-
P450-MKNF2
-
-
-
-
P450-NMB
-
-
-
-
P450-OLF1
-
-
-
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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
-
-
-
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P450H
-
-
-
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P450I
-
-
-
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P450IIC5
-
-
-
-
P450MT2
-
-
-
-
P450RAP
-
-
-
-
P450RLM6
-
-
-
-
P52
-
-
-
-
PB15
-
-
-
-
PHP2
-
-
-
-
PHP3
-
-
-
-
Progesterone 21-hydroxylase
-
-
-
-
Prostaglandin omega-hydroxylase
-
-
-
-
PTF1
-
-
-
-
PTF2
-
-
-
-
S-mephenytoin 4-hydroxylase
-
-
-
-
Steroid hormones 7-alpha-hydroxylase
-
-
-
-
Testosterone 15-alpha-hydroxylase
-
-
-
-
Testosterone 16-alpha hydroxylase
-
-
-
-
Testosterone 6-beta-hydroxylase
-
-
-
-
Testosterone 7-alpha-hydroxylase
-
-
-
-
xenobiotic monooxygenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
desulfation
-
-
-
-
epoxidation
-
-
-
-
hydroxylation
-
-
-
-
N-dealkylation
-
-
-
-
N-oxidation
-
-
-
-
O-dealkylation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction of azo, nitro, N-oxide groups
-
-
-
-
S-dealkylation
-
-
-
-
sulfoxidation
-
-
-
-
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
adrenic acid + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
i.e. all-cis-7,10,13,16-docosatetraenoic acid
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
-
?
aryl hydrocarbons + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
e.g. benzo[a]pyrene, ethoxyresuforin, biphenyl, p-nitroanisole, acetanilide, 2-acetylaminofluorene, 2-ethoxycoumarin, estradiol-17beta, testosterone
-
-
?
docosahexaenoic acid + [reduced NADPH-hemoprotein reductase] + O2
22-hydroxydocosahexaenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
eicosapentaenoic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyeicosapentaenoic acid + [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
-
-
-
-
?
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
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
cytochrome P450-dependent metabolism of omega-6 polyunsaturated fatty acids, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CP2B9_MOUSE
491
1
55741
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2BA_MOUSE
500
1
56744
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2BJ_MOUSE
492
0
55997
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP1A2_MOUSE
513
1
58184
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP237_MOUSE
490
0
55606
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP238_MOUSE
490
0
56229
Swiss-Prot
Secretory Pathway (Reliability: 2)
CP239_MOUSE
490
0
55827
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP254_MOUSE
490
0
55858
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP4B1_MOUSE
511
1
58900
Swiss-Prot
Secretory Pathway (Reliability: 2)
CP4CA_MOUSE
508
0
58350
Swiss-Prot
Secretory Pathway (Reliability: 3)
CP4CB_MOUSE
508
0
58309
Swiss-Prot
Secretory Pathway (Reliability: 3)
CP2CT_MOUSE
490
0
55716
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2D9_MOUSE
504
0
56950
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2DA_MOUSE
504
2
57233
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2DB_MOUSE
504
1
56988
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP1A1_MOUSE
524
1
59230
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2J5_MOUSE
501
1
57784
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2J6_MOUSE
501
2
57792
Swiss-Prot
Secretory Pathway (Reliability: 1)
CY250_MOUSE
490
0
55765
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2DQ_MOUSE
500
2
56976
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2E1_MOUSE
493
1
56805
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP1B1_MOUSE
543
0
60537
Swiss-Prot
Secretory Pathway (Reliability: 5)
CP255_MOUSE
490
0
56096
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP341_MOUSE
504
2
57987
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2A4_MOUSE
494
1
56782
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2A5_MOUSE
494
1
56741
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP2AC_MOUSE
492
1
56179
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP3AB_MOUSE
504
2
57855
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP3AD_MOUSE
503
0
57492
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP3AG_MOUSE
504
1
57870
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP3AP_MOUSE
503
2
58122
Swiss-Prot
Secretory Pathway (Reliability: 1)
D3Z7F1_MOUSE
448
2
49792
TrEMBL
Secretory Pathway (Reliability: 1)
Q9WUD0_MOUSE
491
1
55871
TrEMBL
Secretory Pathway (Reliability: 1)
B6VGH4_MOUSE
513
1
58184
TrEMBL
Secretory Pathway (Reliability: 1)
Q0PGA1_MOUSE
333
1
38172
TrEMBL
Secretory Pathway (Reliability: 1)
A6H6J2_MOUSE
491
1
55846
TrEMBL
Secretory Pathway (Reliability: 1)
G3X8Q9_MOUSE
500
1
56874
TrEMBL
Secretory Pathway (Reliability: 1)
E9Q593_MOUSE
491
1
55859
TrEMBL
Secretory Pathway (Reliability: 1)
B2RXZ2_MOUSE
492
1
56318
TrEMBL
Secretory Pathway (Reliability: 1)
Q9WV19_MOUSE
494
1
56820
TrEMBL
Secretory Pathway (Reliability: 1)
Q91X75_MOUSE
494
1
56713
TrEMBL
Secretory Pathway (Reliability: 1)
F7B9W9_MOUSE
128
0
15080
TrEMBL
other Location (Reliability: 2)
Q80XK1_MOUSE
493
1
56582
TrEMBL
Secretory Pathway (Reliability: 1)
Q8K027_MOUSE
323
1
36066
TrEMBL
other Location (Reliability: 4)
A0A1B0GSV7_MOUSE
434
1
49856
TrEMBL
Secretory Pathway (Reliability: 1)
Q3UEM4_MOUSE
457
1
52207
TrEMBL
Secretory Pathway (Reliability: 1)
Q05A20_MOUSE
524
1
59230
TrEMBL
Secretory Pathway (Reliability: 1)
Q64460_MOUSE
491
1
55760
TrEMBL
Secretory Pathway (Reliability: 1)
Q0PGA0_MOUSE
157
1
17837
TrEMBL
Secretory Pathway (Reliability: 1)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
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