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Information on EC 1.14.14.1 - unspecific monooxygenase and Organism(s) Rattus norvegicus and UniProt Accession P04799

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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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This record set is specific for:
Rattus norvegicus
UNIPROT: P04799
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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
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-
-
-
7-alkoxycoumarin O-dealkylase
-
-
AA omega-hydroxylase
-
-
Aldehyde oxygenase
-
-
-
-
Arachidonic acid epoxygenase
-
-
-
-
aromatase
-
-
-
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aryl hydrocarbon hydroxylase
-
-
-
-
aryl-4-monooxygenase
-
-
-
-
Brain aromatase
-
-
-
-
Clone PF26
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-
-
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Clone PF3/46
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-
-
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Coumarin 7-hydroxylase
-
-
-
-
CYP1A1
CYP1A2
-
-
-
-
CYP1A3
-
-
-
-
CYP2A3
-
-
-
-
CYP2E1
CYP4502F4
-
-
-
-
CYP6B1V1/CYP6B1V2/ CYP6B1V3
-
-
-
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CYP6B3V1/CYP6B3V2
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-
-
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CYP6B4V1/CYP6B4V2
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-
-
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CYP6B5V1
-
-
-
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CYPIA1
-
-
-
-
CYPIA2
-
-
-
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CYPIA4
-
-
-
-
CYPIA5
-
-
-
-
CYPIB1
-
-
-
-
CYPIIA1
-
-
-
-
CYPIIA10
-
-
-
-
CYPIIA11
-
-
-
-
CYPIIA12
-
-
-
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CYPIIA13
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-
-
-
CYPIIA2
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-
-
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CYPIIA3
-
-
-
-
CYPIIA4
-
-
-
-
CYPIIA5
-
-
-
-
CYPIIA6
-
-
-
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CYPIIA7
-
-
-
-
CYPIIA8
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-
-
-
CYPIIA9
-
-
-
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CYPIIB1
-
-
-
-
CYPIIB10
-
-
-
-
CYPIIB11
-
-
-
-
CYPIIB12
-
-
-
-
CYPIIB19
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-
-
-
CYPIIB2
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-
-
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CYPIIB20
-
-
-
-
CYPIIB3
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-
-
-
CYPIIB4
-
-
-
-
CYPIIB5
-
-
-
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CYPIIB6
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-
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CYPIIB9
-
-
-
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CYPIIC1
-
-
-
-
CYPIIC10
-
-
-
-
CYPIIC11
-
-
-
-
CYPIIC12
-
-
-
-
CYPIIC13
-
-
-
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CYPIIC14
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CYPIIC15
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CYPIIC16
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CYPIIC17
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CYPIIC18
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CYPIIC19
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CYPIIC2
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CYPIIC20
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CYPIIC21
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CYPIIC22
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CYPIIC23
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CYPIIC24
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CYPIIC25
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-
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CYPIIC26
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CYPIIC27
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-
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CYPIIC28
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CYPIIC29
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CYPIIC3
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CYPIIC30
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-
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CYPIIC31
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CYPIIC37
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-
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CYPIIC38
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CYPIIC39
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CYPIIC4
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CYPIIC40
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CYPIIC41
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CYPIIC42
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CYPIIC5
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CYPIIC6
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-
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CYPIIC7
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CYPIIC8
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CYPIIC9
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CYPIID1
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CYPIID10
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CYPIID11
-
-
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CYPIID14
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CYPIID15
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CYPIID16
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CYPIID17
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CYPIID18
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-
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CYPIID19
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CYPIID2
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CYPIID3
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CYPIID4
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CYPIID5
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CYPIID6
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CYPIID9
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CYPIIE1
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CYPIIF1
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CYPIIF3
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CYPIIF4
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CYPIIG1
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CYPIIH1
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CYPIIH2
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CYPIIIA1
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CYPIIIA10
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CYPIIIA11
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CYPIIIA12
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CYPIIIA13
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CYPIIIA14
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CYPIIIA15
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CYPIIIA16
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CYPIIIA17
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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
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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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-
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CYPIVF5
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-
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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 P-450 4 enzyme
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cytochrome P450 3A
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cytochrome P450 monooxygenase
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Cytochrome P450-D2
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cytochrome P450-dependent monooxygenase
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DAH1
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DAH2
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Debrisoquine 4-hydroxylase
-
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Estrogen synthetase
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flavoprotein monooxygenase
-
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flavoprotein-linked monooxygenase
-
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Hepatic cytochrome P-450MC1
-
-
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HLp
-
-
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IIA3
-
-
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Isozyme 3A
-
-
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Laurate omega-1 hydroxylase
-
-
-
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Lauric acid omega-6-hydroxylase
-
-
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LMC1
-
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Mephenytoin 4-hydroxylase
-
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microsomal monooxygenase
-
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microsomal P-450
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N-demethylase
-
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O-demethylase
-
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OLF2
-
-
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Olfactive
-
-
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Ovarian aromatase
-
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oxygenase, flavoprotein-linked mono-
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P(3)450
-
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P-448
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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
-
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P-450IIIAM1
-
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P-450MC
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P-450MP
-
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P-450UT
-
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P1-88
-
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P24
-
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P450 17-alpha
-
-
-
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P450 2D-29/2D-35
-
-
-
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P450 CM3A-10
-
-
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P450 DUT2
-
-
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P450 FA
-
-
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P450 FI
-
-
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P450 form 3B
-
-
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P450 form HP1
-
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P450 HSM1
-
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P450 HSM2
-
-
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P450 HSM3
-
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P450 HSM4
-
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P450 IIB1
-
-
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P450 IIC2
-
-
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P450 LM4
-
-
-
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P450 LM6
-
-
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P450 LMC2
-
-
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P450 MD
-
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P450 monooxygenase
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P450 MP-12/MP-20
-
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P450 P49
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P450 PB1
-
-
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P450 PB4
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P450 PBC1
-
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P450 PBC2
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P450 PBC3
-
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P450 PBC4
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P450 PCHP3
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P450 PCHP7
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P450 TCDDAA
-
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P450 TCDDAHH
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P450 type B2
-
-
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P450 types B0 and B1
-
-
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P450(I)
-
-
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P450-11A
-
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P450-15-alpha
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P450-15-COH
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P450-16-alpha
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P450-254C
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P450-3C
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P450-6B/29C
-
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P450-A3
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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
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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
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P450-HP
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P450-IIA10
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P450-IIA11
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P450-IIA3.1
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P450-IIA3.2
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P450-IIA4
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P450-KP1
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P450-LM2
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P450-MC1
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P450-MC4
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P450-MK1
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P450-MKJ1
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P450-MKMP13
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P450-MKNF2
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P450-NMB
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P450-OLF1
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P450-OLF3
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P450-P1
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P450-P2/P450-P3
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P450-P3
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P450-PB1 and P450-PB2
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P450-PCN1
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P450-PCN2
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P450-PCN3
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P450-PM4
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P450-PP1
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P450-PROS2
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P4501A1
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P450CB
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P450CMEF
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P450E
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P450EF
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P450F
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P450H
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P450I
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P450IIC5
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P450MT2
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P450RAP
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P450RLM6
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P450s 3A
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P52
-
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PB15
-
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PHP2
-
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PHP3
-
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Progesterone 21-hydroxylase
-
-
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Prostaglandin omega-hydroxylase
-
-
-
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PTF1
-
-
-
-
PTF2
-
-
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S-mephenytoin 4-hydroxylase
-
-
-
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sertraline N-demethylase
-
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Steroid hormones 7-alpha-hydroxylase
-
-
-
-
Testosterone 15-alpha-hydroxylase
-
-
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-
Testosterone 16-alpha hydroxylase
-
-
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Testosterone 6-beta-hydroxylase
-
-
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-
Testosterone 7-alpha-hydroxylase
-
-
-
-
xenobiotic monooxygenase
-
-
-
-
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
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
okadaic acid + NADPH + O2
?
show the reaction diagram
-
-
-
?
6beta-hydroxytestosterone + [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 CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
-
?
7-ethoxyresorufin + O2 + reduced donor
?
show the reaction diagram
-
7-ethoxyresorufin O-deethylation
-
-
?
7-hydroxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
-
?
7-propoxycoumarin + [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
-
-
?
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
20-hydroxyeicosatetraenoic acid + 19-hydroxyeicosatetraenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
ratio 12:1
-
?
aryl hydrocarbons + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
prostaglandins
-
-
?
benzo-pyrene + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
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
-
-
?
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 + 19-hydroxyeicosapentaenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
ratio 4:3
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
(9Z,12Z)-18-hydroxyoctadeca-9,12-dienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
okadaic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
-
-
-
?
p-nitrophenol + [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
-
-
?
tolbutamide + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
vandetanib + [reduced NADPH-hemoprotein reductase] + H+ + O2
N-desmethylvandetanib + [oxidized NADPH-hemoprotein reductase] + ?
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
7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2
7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
show the reaction diagram
-
wild-type enzyme and recombinant enzyme CYP1A1 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
-
?
benzo-pyrene + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
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
-
-
?
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
NADH
when NADH is used together with NADPH in the incubation mixture, CYP2C11 produces up to 1.2times higher levels of N-desmethylvandetanib
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
heme iron
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bitertanol
-
7-ethoxyresorufin O-deethylation is inhibited by the fungicide bitertanol, IC50: 800-900 nM
N-benzoloxycarbonyl-Leu-Leu-leucinal
-
MG132, high concentrations are cytotoxic and can suppress CYP3A synthesis. Biphasic concentration effect on CYP3A turnover: stabilization at 0.005 to 0.01 mM with marked suppression at more than 0.1 mM. Marked (approximately 4fold) MG132 concentration-dependent RNA-dependent protein kinase-like ER-bound elF2alpha-kinase autophosphorylation, along with an 8fold increase in elF2alpha-phosphorylation. In parallel, MG132 also activates general control nonderepressible-2 elF2alpha kinase in a concentration-dependent manner, but not the heme-regulated inhibitor elF2alpha kinase. Consequently dramatic translational shutoff of total hepatic protein, including but not limited to CYP3A and tryptophan 2,3-dioxygenase protein syntheses
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the enzyme is induced and inhibited by the fungicide bitertanol, application increases the activiy of several cytochrome P450 monooxygenases in liver, kidney, and lung several fold, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008 - 0.0009
bitertanol
Rattus norvegicus
-
7-ethoxyresorufin O-deethylation is inhibited by the fungicide bitertanol, IC50: 800-900 nM
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
isozyme tissue-specific expression analysis, regulation by PPAR
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
metabolism of okadaic acid to oxygenated metabolites correlates with detoxification by Cyp3A enzymes. The okadaic acid toxicity is enhanced in the presence of rat CYP1A2
metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CP1A2_RAT
513
1
58259
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 50000-52000, CYP4A isoforms, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of a fused enzyme between rat CYP1A1 and rat reductase on microsomes in the recombinant yeast cells, which showed enhanced specific activity as compared with the original enzyme system
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially by microsome preparation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HepG2 cells
expression anbalysis at restricted feeding versus ad libitum
-
expression in HepG2 cells
functional expression of the fused enzyme between rat CYP1A1 and rat or yeast reductase in transgenic tobacco and potato plants mainly in microsomes
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
beta-naphthoflavone (0.05 mM) causes a 71fold increase in CYP1A2-dependent activity and a 253fold increase in CYP1A2 mRNA expression in hepatocyte microsomes
in hepatocyte cultures, treatment with 0.05 mM Andrographis paniculata extract and Andrographolide results in a 60% decrease in CYP1A2 expression and activity
dexamethasone (0.05 mM) and rifampicin (0.01 mM) increase CYP2C11 activity by a mean of 1.4fold in hepatocytes
dexamethasone (0.05 mM) increases CYP3A1 activity by a mean of 6fold and dexamethasone (0.05 mM) and rifampicin (0.01 mM) increase CYP3A1 mRNA expression by a mean of 167fold in hepatocytes
dexamethasone-mediated CYP3A induction
-
in hepatocyte cultures, treated with 0.05 mM Andrographis paniculata extract and Andrographolide, CYP2E1 is not significantly decreased (by 30%)
in hepatocyte cultures, treatment with 0.05 mM Andrographis paniculata extract and Andrographolide results in a 50% decrease in CYP3A1 expression and activity
in hepatocyte cultures, treatment with 0.05 mM Andrographis paniculata extract and Andrographolide results in a 60% decrease in CYP2C11 expression and activity. After in vivo administration, Andrographis paniculata extract at dose levels of 0.5 g/kg/day (i.e. 5 mg/kg/day Andrographolide equivalents) and at 2.5 g/kg/day (i.e. 25 mg/kg/day Andrographolide equivalents) and Andrographolide at dose levels of 5 and 25 mg/kg/day significantly decrease CYP2C11 activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
2fold increase in enzyme activity on diet of total parenteral nutrition plus choline
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
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
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.
44
2047-2057
2006
Rattus norvegicus
Manually annotated by BRENDA team
Hirao, J.; Arakawa, S.; Watanabe, K.; Ito, K.; Furukawa, T.
Effects of restricted feeding on daily fluctuations of hepatic functions including P450 monooxygenase activities in rats
J. Biol. Chem.
281
3165-3171
2006
Rattus norvegicus
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
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
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.
76
503-515
2009
Rattus norvegicus
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
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
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)
Manually annotated by BRENDA team