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Information on EC 1.14.14.94 - leukotriene-B4 20-monooxygenase and Organism(s) Homo sapiens and UniProt Accession P78329
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1.14.14.94 leukotriene-B4 20-monooxygenaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein found in mammals.
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Word Map
- 1.14.14.94
- warfarin
- vkorc1
- cyp2c9
-
anticoagulant
-
arachidonic
-
dosing
-
pharmacogenetic
- 20-hete
-
20-hydroxyeicosatetraenoic
- cyp4fs
- cyp4a11
-
omega-hydroxylation
- epoxide
-
eicosanoids
- cyp3a5
-
interindividual
-
acenocoumarol
-
pharmacogenomics
-
thromboembolic
-
non-genetic
- cyp1b1
-
omega-oxidation
-
17-octadecynoic
-
epoxyeicosatrienoic
-
pharmacogenes
-
genotype-guided
-
lipoxins
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyp4f2, cyp4f3, cyp4f12, cyp4f11, cyp4f8, cyp4f3b, ltb4 omega-hydroxylase, cytochrome p450 4f2, cyp4f3a, cyp4f4, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP4F3
CYPIVF2
-
-
-
-
CYPIVF3
-
-
-
-
Cytochrome P450-LTB-omega
-
-
-
-
leukotriene B4 20-hydroxylase
-
-
-
-
Leukotriene-B4 20-monooxygenase
-
-
-
-
leukotriene-B4 omega-hydroxylase
-
-
-
-
LTB4 20-hydroxylase
-
-
-
-
LTB4 omega-hydroxylase
oxygenase, leukotriene B4 20-mono-
-
-
-
-
CYP4F3
CYP4F3 undergoes tissue-specific alternative splicing to CYP4F3A and CYP4F3B
LTB4 omega-hydroxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
reduction
-
-
-
-
omega-oxidation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (20-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein found in mammals.
CAS REGISTRY NUMBER
COMMENTARY
90119-11-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
(E,Z,Z,Z)-8-hydroxy-5,9,11,14-eicosatetraenoic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F2
-
-
?
(Z12(13))-epoxyoctadec-(Z9)-enoic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
(Z12(13))-epoxyoctadec-Z9-enoic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
(Z9(10))-epoxyoctadec-(Z12)-enoic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
(Z9(10))-epoxyoctadec-Z12-enoic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
(Z9(10))-epoxyoctadecanoic acid + NADPH + O2
?
-
omega-hydroxylation activity and weak (omega-1)-hydroxylation activity
-
-
?
12-hydroxyeicosatetraenoic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F3A
-
-
?
20-hydroxy-leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F3
-
-
?
20-hydroxy-leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
5-deoxy-leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
5-deoxy-20-hydroxy-leukotriene B4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
5-epi-leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
5-epi-20-hydroxy-leukotriene B4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
5-hydroxy-6,8,11,14-eicosatetraenoic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F3
-
-
?
6-trans-12-epi-leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
6-trans-12-epi-20-hydroxy-leukotriene B4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
9,11-diazo-15-deoxy-prostaglandin H2 + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F8
-
-
?
9,11-epoxymethano-prostaglandin H2 + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F8
-
-
?
alpha-tocopherol + [reduced NADPH-hemoprotein reductase] + O2
alpha-13'-hydroxy-tocopherol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
arachidonate + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-5,8,11,14-eicosatetraenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
18(R)-hydroxyarachidonate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
delta-tocopherol + [reduced NADPH-hemoprotein reductase] + O2
delta-13'-hydroxy-tocopherol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
gamma-tocopherol + [reduced NADPH-hemoprotein reductase] + O2
13'-hydroxy-gamma-tocopherol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-leukotriene B4 + [oxidized NADPH-hemoprotein reductase] + H2O
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
?
-
induction of in all-trans-retinoic acid-treated HL60 cells
-
-
?
prostaglandin H1 + [reduced NADPH-hemoprotein reductase] + O2
19-hydroxy-prostaglandin H1 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4F8
-
-
?
prostaglandin H2 + [reduced NADPH-hemoprotein reductase] + O2
19-hydroxy-prostaglandin H2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4F8
-
-
?
(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
inactivation of leukotriene B4, a mediator of inflammation
-
-
?
12-hydroxy-5,8,10,14-eicosatetraenoic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
12-hydroxy-5,8,10,14-eicosatetraenoic acid + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F2
-
-
?
6-trans-leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F2
-
-
?
6-trans-leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F3
-
-
?
6-trans-leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F3A
-
-
?
arachidonate + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-5,8,11,14-eicosatetraenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
arachidonate + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-5,8,11,14-eicosatetraenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
very poor substrate
-
-
?
arachidonate + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-5,8,11,14-eicosatetraenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is the principal arachidonate omega-hydroxylase in liver, CYP4F2
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4F3A is expressed in human leukocytes and catalyzes the omega-hydroxylation of LTB4
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4F3A catalyzes the omega-hydroxylation of LTB4
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-leukotriene B4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-leukotriene B4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
leukotriene B4 is identical with (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-leukotriene B4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme plays a critical role in regulating the biological effect of leukotriene B4, CYP4F3
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-leukotriene B4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
yielding omega-COOH-leukotriene B4 via omega-hydroxy-leukotriene B4 and omega-CHO-leukotriene B4, CYP4F3
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-leukotriene B4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
all recombinant proteins generate product I from leukotriene B4, which in all cases is indistinguishable from the 20-hydroxy-leukotriene B4 reference compound assayed under similar conditions. CYP4F3A is the most efficient leukotriene B4 20-hydroxylase. CYP4F3A and 4F3B generate a secondary product, which is 20-COOH leukotriene B4 derived from 20-hydroxy-leukotriene B4. CYP4F12 is least efficient, generating several additional products. Product I derived from CYP4F3A and that from epidermal keratinocytes are identical to the 20-hydroxy-leukotriene B4 reference compound
-
-
?
lipoxin A4 + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F3 preferentially omega-jydroxylates lipoxin B4 over lipoxin A4
-
-
?
lipoxin A4 + [reduced NADPH-hemoprotein reductase] + O2
?
-
no omega-hydroxylation of LXB4, CYP4F2
-
-
?
lipoxin B4 + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP4F3 preferentially omega-jydroxylates lipoxin B4 over lipoxin A4
-
-
?
additional information
?
-
cytochrome P450 4F2 gene encodes for the major CYP enzyme responsible for the synthesis of 20-hydroxyeicosatetraenoic acid in the human kidney
-
-
?
additional information
?
-
-
cytochrome P450 4F2 gene encodes for the major CYP enzyme responsible for the synthesis of 20-hydroxyeicosatetraenoic acid in the human kidney
-
-
?
additional information
?
-
-
overview, stereochemical requirement for substrate specificity
-
-
?
additional information
?
-
-
recombinant protein CYP4F3, wide substrate specificity
-
-
?
additional information
?
-
-
CYP4F3B and CYP4F2 may function collaboratively as 20-HETE synthetase as well as omega-hydroxylases for leukotiene b4 and other lipoxygenase-dependent eicosanoids in human liver and other tissues
-
-
?
additional information
?
-
-
no activity with 20-hydroxy-leukotriene B4 and lipoxin B4
-
-
?
additional information
?
-
-
leukotriene B4 and arachidonate omega-hydroxylase activities are both CYP4F2-catalyzed in the liver, overview
-
-
?
additional information
?
-
-
CYP4F3A also catalyzes the omega-hydroxylation of epoxyeicosatrieonic acids
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
arachidonate + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-5,8,11,14-eicosatetraenoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is the principal arachidonate omega-hydroxylase in liver, CYP4F2
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4F3A is expressed in human leukocytes and catalyzes the omega-hydroxylation of LTB4
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy-leukotriene B4 + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme plays a critical role in regulating the biological effect of leukotriene B4, CYP4F3
-
-
?
leukotriene B4 + [reduced NADPH-hemoprotein reductase] + O2
?
-
induction of in all-trans-retinoic acid-treated HL60 cells
-
-
?
(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + [reduced NADPH-hemoprotein reductase] + O2
(6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
inactivation of leukotriene B4, a mediator of inflammation
-
-
?
additional information
?
-
cytochrome P450 4F2 gene encodes for the major CYP enzyme responsible for the synthesis of 20-hydroxyeicosatetraenoic acid in the human kidney
-
-
?
additional information
?
-
-
cytochrome P450 4F2 gene encodes for the major CYP enzyme responsible for the synthesis of 20-hydroxyeicosatetraenoic acid in the human kidney
-
-
?
additional information
?
-
-
CYP4F3B and CYP4F2 may function collaboratively as 20-HETE synthetase as well as omega-hydroxylases for leukotiene b4 and other lipoxygenase-dependent eicosanoids in human liver and other tissues
-
-
?
additional information
?
-
-
leukotriene B4 and arachidonate omega-hydroxylase activities are both CYP4F2-catalyzed in the liver, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
all-trans retinoic acid
-
significantly induces expression of CYP4F3A at both mRNA and protein levels in cultured HL-60 cells
lipopolysaccharide
-
upregulates expression and activity of LTB4OH in ex-smokers in a dose-dependent manner, but not in smokers. In vitro smoke exposure of ex-smokers' bronchoalveolar lavage cells abrogates the lipopolysaccharide-induced up-regulation of LTB4OH mRNA expression, thus tobacco smoke alters bronchoalveolar lavage cell LTB4OH mRNA expression in response to lipopolysaccharide exposure
phenol
-
significantly induces expression of CYP4F3A at both mRNA and protein levels in cultured and differentiated HL-60 cells, in the proerythroid cell line K-562, and ex vivo in human neutrophils
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 9.5
-
pH 6.8: about 50% of activity maximum, pH 9.5: about 70% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
ex-smokers express significantly higher LTB4OH mRNA levels than smokers
-
exhibits greater leukotriene B4 hydroxylase activities than fresh skin tissues of either species
-
CYP4F3 is specifically expressed in. CYP4F3 is restricted to myeloid cells
additional information
additional information
-
CYP4F2 is not expressed in myeloid cells, polymorphonuclear leukocyte
additional information
-
tissue-specific expression and function of CYP4F2, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
CYP4F catalyzes the omega-hydroxylation of the side chain of tocopherols and tocotrienols, the first step in their catabolism to polar metabolites excreted in urine. CYP4F2 is the only enzyme currently shown to metabolize vitamin E in humans
physiological function
physiological function
-
by regulating the balance of leukotriene B4 in the lung, LTB4OH may function as a suppressor of lung carcinogenesis
physiological function
-
is critical in the inactivation of leukotriene B4 in polymorphonuclear leukocytes with a -fold induction between 3 and 71
physiological function
CYP4F3B plays a central role in the inactivation and elimination of leukotrienes from systemic circulation during the resolution of inflammation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CP4F2_HUMAN
520
1
59853
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
61000
-
recombinant isoforms CYP4F3A and CYP4F3B expressed in COS-7 cells, western blot analysis
additional information
-
the isolated cDNA encodes a protein of 520 amino acids with 59805 Da, CYP4F3
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V433M
the functional polymorphism in human Cyp4F2 decreases 20-hydroxyeicosatetraenoic acid production, but does not influence the omega-hydroxylation of leukotriene B4, screening and genotyping of African and European Americans, overview
W12G
the mutant enzyme activity is similar to the wild-type enzyme, screening and genotyping of African and European Americans, overview
W12G/V433M
the functional polymorphism in human Cyp4F2 decreases 20-hydroxyeicosatetraenoic acid production, but does not influence the omega-hydroxylation of leukotriene B4, screening and genotyping of African and European Americans, overview
V433M
-
naturally occuring common genetic variant of the human CYP4F2 gene, the mutant has lower enzyme specific activity toward tocopherols, 42-66% of wild-type activity, but is without a significant effect on the metabolism of tocotrienols
W12G
-
naturally occuring common genetic variant of the human CYP4F2 gene, the mutant exhibits a greater enzyme specific activity compared to the wild-type enzyme for both tocopherols and tocotrienols, 230-275% of wild-type activity towards alpha, gamma, and delta-tocopherol and 350% of wild-type activity towards alpha, gamma, and delta-tocotrienol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, no loss of activity with highly purified preparations even after 4 years
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from insect Sf9 suspension cultures, to near homogeneity, native enzyme partially from liver and kidney by microsome preparation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant DNA and amino acid sequence determinations, functional nonsynonymous polymorphisms, overview, expression of wild-type and mutant genes in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method
expression in Spodoptera frugiperda Sf9 cells using the baculovirus infection system
-
expression of wild-type and CYP4F2 mutant enzymes in Spodoptera frugiperda SF9 insect cell microsomes via the baculovrius transfection system
-
tissue-specific expression is regulated by alternative promoter usage and mutually exclusive exon splicing, exon 3 and 4
-
two isoforms of CYP4F3, CYP4F3A expressed in neutrophils and CYP4F3B expressed in fetal and adult liver
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
induction of CYP4F3 may play a role in the development of benzene hematotoxicity and serve as a biomarker of benzene exposure
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Soberman, R.J.; Harper, T.W.; Murphy, R.C.; Austen, K.F.
Identification and functional characterization of leukotriene B4 20-hydroxylase of human polymorphonuclear leukocytes
Proc. Natl. Acad. Sci. USA
82
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1985
Homo sapiens
Powell, W.S.
Properties of leukotriene B4 20-hydroxylase from polymorphonuclear leukocytes
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259
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1984
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Shak, S.; Reich, N.O.; Goldstein, I.M.; Ortiz de Montellano, P.R.
Leukotriene B4 omega-hydroxylase in human polymorphonuclear leukocytes. Suicidal inactivation by acetylenic fatty acids
J. Biol. Chem.
260
13023-13028
1985
Homo sapiens
Soberman, R.J.; Okita, R.T.; Fitzsimmons, B.; Rokach, J.; Spur, B.; Austen, K.F.
Stereochemical requirements for substrate specificity of LTB4 20-hydroxylase
J. Biol. Chem.
262
12421-12427
1987
Homo sapiens
Soberman, R.J.; Okita, R.T.
Leukotriene B4 20-hydroxylase of human polymorphonuclear leukocytes
Methods Enzymol.
163
349-353
1988
Homo sapiens
Sumimoto, H.; Takeshige, K.; Minakami, S.
Characterization of human neutrophil leukotriene B4 omega-hydroxylase as a system involving a unique cytochrome P-450 and NADPH-cytochrome P-450 reductase
Eur. J. Biochem.
172
315-324
1988
Homo sapiens
Christmas, P.; Ursino, S.R.; Fox, J.W.; Soberman, R.J.
Expression of the CYP4F3 gene. Tissue-specific splicing and alternative promoters generate high and low Km forms of leukotriene B4.omega-hydroxylase
J. Biol. Chem.
274
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1999
Homo sapiens
Ikehata, A.; Hiwatashi, N.; Kinouchi, Y.; Ito, K.; Yamazaki, H.; Toyota, T.
5-Aminosalicylic acid inhibits leukotriene B4 omega-hydroxylase activity in human polymorphonuclear leukocytes
Prostaglandins Leukot. Essent. Fatty Acids
50
317-320
1994
Homo sapiens
Kikuta, Y.; Kusunose, E.; Sumimoto, H.; Mizukami, Y.; Takeshige, K.; Sakaki, T.; Yabusaki, Y.; Kusunose, M.
Purification and characterization of recombinant human neutrophil leukotriene B4 omega-hydroxylase (cytochrome P450 4F3)
Arch. Biochem. Biophys.
355
201-205
1998
Homo sapiens
Kikuta, Y.; Miyauchi, Y.; Kusunose, E.; Kusunose, M.
Expression and molecular cloning of human liver leukotriene B4 omega-hydroxylase (CYP4F2) gene
DNA Cell Biol.
18
723-730
1999
Homo sapiens
Kikuta, Y.; Kusunose, E.; Kusunose, M.
Characterization of human liver leukotriene B4 omega-hydroxylase P450 (CYP4F2)
J. Biochem.
127
1047-1052
2000
Homo sapiens
Mizukami, Y.; Sumimoto, H.; Takeshige, K.
Induction of cytochrome CYP4F3A in all-trans-retinoic acid-treated HL60 cells
Biochem. Biophys. Res. Commun.
314
104-109
2004
Homo sapiens
Kikuta, Y.; Kusunose, E.; Kusunose, M.
Catalytic properties of two human leukotriene B4 omega-hydroxylase P450s
Int. Congr. Ser.
1233
139-142
2002
Homo sapiens
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le Quere, V.; Plee-Gautier, E.; Potin, P.; Madec, S.; Salaun, J.P.
Human CYP4F3s are the main catalysts in the oxidation of fatty acid epoxides
J. Lipid Res.
45
1446-1458
2004
Homo sapiens
Kikuta, Y.; Kusunose, E.; Kusunose, M.
Prostaglandin and leukotriene omega-hydroxylases
Prostaglandins
68-69
345-362
2002
Homo sapiens
Hirani, V.; Yarovoy, A.; Kozeska, A.; Magnusson, R.P.; Lasker, J.M.
Expression of CYP4F2 in human liver and kidney: Assessment using targeted peptide antibodies
Arch. Biochem. Biophys.
478
59-68
2008
Homo sapiens
Kikuta, Y.; Mizomoto, J.; Strobel, H.W.; Ohkawa, H.
Expression and physiological function of CYP4F subfamily in human eosinophils
Biochim. Biophys. Acta
1771
1439-1445
2007
Homo sapiens
Stec, D.E.; Roman, R.J.; Flasch, A.; Rieder, M.J.
Functional polymorphism in human CYP4F2 decreases 20-HETE production
Physiol. Genomics
30
74-81
2007
Homo sapiens (P78329), Homo sapiens
Du, L.; Yin, H.; Morrow, J.D.; Strobel, H.W.; Keeney, D.S.
20-Hydroxylation is the CYP-dependent and retinoid-inducible leukotriene B4 inactivation pathway in human and mouse skin cells
Arch. Biochem. Biophys.
484
80-86
2009
Homo sapiens, Mus musculus, Mus musculus CD-1
Mao, J.T.; Tashkin, D.P.; Tsu, I.H.; Serio, K.J.
Differential modulation of leukotriene B4 synthesis and degradation in human bronchoalveolar lavage cells by lipopolysaccharide and tobacco smoke
Cancer Prev. Res. (Phila)
1
266-274
2008
Homo sapiens
Zhao, Z.; He, X.; Bi, Y.; Xia, Y.; Tao, N.; Li, L.; Ma, Q.
Induction of CYP4F3 by benzene metabolites in human white blood cells in vivo in human promyelocytic leukemic cell lines and ex vivo in human blood neutrophils
Drug Metab. Dispos.
37
282-291
2009
Homo sapiens
Bardowell, S.A.; Stec, D.E.; Parker, R.S.
Common variants of cytochrome P450 4F2 exhibit altered vitamin E-omega-hydroxylase specific activity
J. Nutr.
140
1901-1906
2010
Homo sapiens
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