Information on EC 1.14.14.80 - long-chain fatty acid omega-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.80
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RECOMMENDED NAME
GeneOntology No.
long-chain fatty acid omega-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain fatty acid + [reduced NADPH-hemoprotein reductase] + O2 = an omega-hydroxy-long-chain fatty acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cutin biosynthesis
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sophorolipid biosynthesis
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sporopollenin precursors biosynthesis
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suberin monomers biosynthesis
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Fatty acid degradation
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Cutin, suberine and wax biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
long-chain fatty acid,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (omega-hydroxylating)
The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (omega-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
white-tufted-ear marmoset
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
formerly Candida bombicola
B8QHP1, B8QHP3, B8QHP5
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
9,10-epoxystearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxy-9,10-epoxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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-
-
?
alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy arachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
cis-9,10-epoxystearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxy-cis-9,10-epoxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
B8QHP1;, B8QHP3;, B8QHP5;
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-
-
?
inoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
B8QHP1;, B8QHP3;, B8QHP5;
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-
-
?
isolauric acid + [reduced NADPH-hemoprotein reductase] + O2
11-hydroxyisolauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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-
-
-
?
isomyristic acid + [reduced NADPH-hemoprotein reductase] + O2
13-hydroxyisomyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
lauric acid + [reduced NADPH-hemoprotein reductase] + O2+ O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
best substrate
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-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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CYP4V2 is a selective omega-hydroxylase of saturated, medium-chain fatty acids with relatively high catalytic efficiency toward myristic acid
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-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyrisitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
B8QHP1;, B8QHP3;, B8QHP5;
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-
-
?
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
stearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
B8QHP1;, B8QHP3;, B8QHP5;
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-
-
?
trans-9,10-epoxystearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxy-trans-9,10-epoxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
B8QHP1;, B8QHP3;, B8QHP5;
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-
-
?
tridecanoic acid + [reduced NADPH-hemoprotein reductase] + O2
13-hydroxytridecanoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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-
-
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?
undecanoic acid + [reduced NADPH-hemoprotein reductase] + O2
11-hydroxyundecanoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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-
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
lauric acid + [reduced NADPH-hemoprotein reductase] + O2+ O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyrisitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
B8QHP1, B8QHP3, B8QHP5
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-
-
?
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
stearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
B8QHP1, B8QHP3, B8QHP5
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-N'-(4-butyl-2-methylphenyl)-N-hydroxyformimidamide
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HET0016
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b5
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.25
arachidonic acid
0.019 - 0.14
lauric acid
0.068
linoleic acid
0.004 - 0.07
myristic acid
0.018 - 0.136
oleic acid
0.014 - 0.43
palmitic acid
additional information
additional information
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Michaelis-Menten kinetics, fatty acids binding constants
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.1
arachidonic acid
0.117 - 10.8
lauric acid
0.1 - 3.8
myristic acid
0.01 - 0.02
oleic acid
0.002 - 1
palmitic acid
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.16 - 30.24
lauric acid
6.04 - 13.52
myristic acid
2.5 - 8.21
palmitic acid
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000038
(E)-N'-(4-butyl-2-methylphenyl)-N-hydroxyformimidamide
Homo sapiens;
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.7
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substrate undecanoic acid, omega-1-hydroxylation, in nmol/min/nmol, pH 7.5, 37°C
1
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substrate lauric acid, omega-1-hydroxylation, in nmol/min/nmol, pH 7.5, 37°C
3
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substrate tridecanoic acid, omega-1-hydroxylation, in nmol/min/nmol, pH 7.5, 37°C
8.5
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substrate tridecanoic acid, omega-hydroxylation, in nmol/min/nmol, pH 7.5, 37°C
12
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substrate undecanoic acid, omega-hydroxylation, in nmol/min/nmol, pH 7.5, 37°C
13.9
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substrate isomyristic acid, omega-hydroxylation, in nmol/min/nmol, pH 7.5, 37°C
14.8
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substrate lauric acid, omega-hydroxylation, in nmol/min/nmol, pH 7.5, 37°C
24.5
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substrate isolauric acid, omega-hydroxylation, in nmol/min/nmol, pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
30
B8QHP1;, B8QHP3;, B8QHP5;
assay at; assay at
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
CYP704B1 is expressed in the developing anthers
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
; CYP86A2 transcripts are 2- to 10fold less abundant in seedling roots, mature roots, and flower; CYP86A8 transcripts are 2fold more abundant in flowers than in seedling shoots; highest expression
Manually annotated by BRENDA team
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cultured hepatocyte
Manually annotated by BRENDA team
CYP86A2 transcripts are 2- to 10fold less abundant in seedling roots, mature roots, and flower; isoform CYP86A1 transcripts are 20fold more abundant in mature roots than in seedling roots
Manually annotated by BRENDA team
older rosettes, low expression
Manually annotated by BRENDA team
abundant expression in seedling shoots; isoform CYP86A1, transcripts are 17fold more abundant in seedling roots than in seedling shoots; shoot and root, low expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
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x * 52000, SDS-PAGE, x * 59347, calculated
55000
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by Coomassie staining and by immunoblotting
59347
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x * 52000, SDS-PAGE, x * 59347, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of active site model. Hydrophobicity in the heme binding site is very different between active and inactive isoforms. CYP94C1 contains highly hydrophobic residues while inactive isoforms CYP704A2 and CYP711A1 do not
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by isolation of microsomes; native enzyme partially by isolation of microsomes; native enzyme partially by isolation of microsomes
B8QHP1;, B8QHP3;, B8QHP5;
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed from pFastbacCYP4V2HIS vector in Escherichia coli DH10Bac. Hexahistidine-tagged CYP4V2 is expressed in Sf-9 cells after infection with the recombinant baculovirus
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expression in COS-7 cells
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expression in Escherichia coli
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expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
expression in Saccharomyces cerevisiae
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expression in Saccharomyces cerevisiae strain WAT11
expression in yeast WAT11 cells
gene CYP4A11, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli
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gene CYP52E3, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae strains WAT11 and and INVSc1; gene CYP52M1, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae strains WAT11 and and INVSc1. 17-Hydroxy linoleic acid is detected in addition to 18-carboxy linoleic acid (cis-9, cis-12-octadecadien-1,18-dioic acid) in the reaction mixture of linoleic acid with CYP52M1-transformed cells; gene CYP52N1, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae strains WAT11 and and INVSc1
B8QHP1;, B8QHP3;, B8QHP5;
gene CYPP4504A11, located on chromosome 7, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time RT PCR enzyme expression analysis, recombinant expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CYP704B1 is highly coexpressed with CYP703A2, a cytochrome P450 involved in exine production
CYP86A1 transcripts are repressed 2.4fold by 27h of iodoacetc acid treatment and5.9fold by 27 h of salicylic acid treatment; CYP86A4 transcripts are repressed 9.0fold by short-term treatment with 1-aminocyclopropane-1-carboxylic acid and induced 1.9fold by long-term treatment with 1-aminocyclopropane-1-carboxylic acid. CYP86A4 transcripts are repressed 3.6fold by 3 h of wounding and 2.4fold in etiolated seedlings; CYP86A7 transcripts are significantly repressed by 2 h of drought treatment, 3 h of salicylic acid and wounding treatments, 3 and 27 h of 1-aminocyclopropane-1-carboxylic acid and mannitol treatments, and in both etiolated and dark-adapted seedlings; CYP86A8 transcripts are repressed by 30 min of wounding
CYP86A2 transcripts are transiently induced 2.5fold by 3 h of wounding and abscisic acid treatment, 2.3fold by 3 h of mannitol treatment, 1.7fold by 3 h of iodoacetic acid treatment, 1.6fold by 3 h of clofibrate treatment, more continuously induced 2.0- and 1.9fold by 30 and 120 min of drought treatment, and induced 1.9- to 2.3fold in etiolated and dark-adapted seedlings; CYP86A4 transcripts are induced 1.9fold by long-term treatment with 1-aminocyclopropane-1-carboxylic acid and repressed 9.0fold by short-term treatment with 1-aminocyclopropane-1-carboxylic acid; CYP86A7 transcripts are transiently induced 1.9fold by 3 h of clofibrate treatment, more continuously induced 1.6 and 1.5fold by 3 and 27 h of methyl jasmonate treatment, and slowly induced 1.7fold by 27 h abscisic acid treatment; CYP86A8 transcripts are induced by 3-h iodoacetic acid and abscisic acid treatments
in ciprofibrate-treated cells, CYP4A expression increases by 1.5- to 1.8fold
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isoform CYP52M1 is clearly upregulated during sophorolipid synthesis
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F434S
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allelic variant, 36% decrease in vamx
G130S
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allelic variant, almost inactive
L509S
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allelic variant, 2.2fold increase in Km
P428L
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allelic variant, almost inactive
V185F
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allelic variant, 4fold increase in Km, 88% decrease in vamx
Y152N
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allelic variant, 95% decrease in vmax
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine