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9,10-epoxystearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxy-9,10-epoxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxy arachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
cis-9,10-epoxystearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxy-cis-9,10-epoxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
isolauric acid + [reduced NADPH-hemoprotein reductase] + O2
11-hydroxyisolauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
isomyristic acid + [reduced NADPH-hemoprotein reductase] + O2
13-hydroxyisomyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
lauric acid + [reduced NADPH-hemoprotein reductase] + O2 + H+
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
best substrate
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP4V2 is a selective omega-hydroxylase of saturated, medium-chain fatty acids with relatively high catalytic efficiency toward myristic acid
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
stearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
trans-9,10-epoxystearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxy-trans-9,10-epoxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
tridecanoic acid + [reduced NADPH-hemoprotein reductase] + O2
13-hydroxytridecanoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
undecanoic acid + [reduced NADPH-hemoprotein reductase] + O2
11-hydroxyundecanoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
?
-
alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
low activity
-
-
?
alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
low activity
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 2.4:1
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 2:1
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 6:1
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
16% of the activity with palmitic acid
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
28% yield
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
substrate for isoforms CYP86A1, CYP86A2, CYP86A4, CYP86A7, CYP86A8
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 2.5:1
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 2.5:1
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 3:1
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 40:1
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 6:1
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
52% of the activity with palmitic acid
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
28% yield
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
49% of the activity with palmitic acid
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 1.6:1
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 1.2:1
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 1.6:1
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 3:1
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
28% yield
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
61% of the activity with palmitic acid
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
best substrate
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
best substrate
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
21% yield
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
28% yield
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 1.6:1
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 1.6:1
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
regioselectivity of omega:omega-1 hydroxylation is 1:1
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
44% yield
-
-
?
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
?
-
isoform CYP86A1 catalyze the omega-hydroxylation of saturated and unsaturated fatty acids with chain lengths from C12 to C18 but not of hexadecane
-
-
?
additional information
?
-
no substrate palmitoyl-CoA
-
-
?
additional information
?
-
no substrate: 12-hydroxylauric acid, lauric acid, cinnamate, p-coumarate, ferulate, sinapate, and p-coumaroyl shikimate
-
-
?
additional information
?
-
Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes
-
-
?
additional information
?
-
the enzyme sequence contains consensus sequences of six substrate recognition sites. Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes. CYP4A11 hydroxylates fatty acids at their omega and omega-1 positions
-
-
?
additional information
?
-
-
octanoic acid is not detectably omega-hydroxylated by CYP4V2
-
-
?
additional information
?
-
isoform CYP4A11 catalyzes the omega- and omega-1-hydroxylation of various fatty acids
-
-
?
additional information
?
-
substrate and product binding and release are much faster than overall rates of catalysis. Both the transfer of an electron to the ferrous-O2 complex and C-H bond-breaking limit the rate of P450 4A11 omega-oxidation
-
-
?
additional information
?
-
-
substrate and product binding and release are much faster than overall rates of catalysis. Both the transfer of an electron to the ferrous-O2 complex and C-H bond-breaking limit the rate of P450 4A11 omega-oxidation
-
-
?
additional information
?
-
isoform CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than alpha-linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega- and omega-1 positions. No activity is detected toward short-chain fatty acids (C10 to C14), cis-11-eicosenoic acid (C20:1), and C16 to C18 alkanes
-
-
?
additional information
?
-
isoform CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than alpha-linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega- and omega-1 positions. No activity is detected toward short-chain fatty acids (C10 to C14), cis-11-eicosenoic acid (C20:1), and C16 to C18 alkanes
-
-
?
additional information
?
-
isoform CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than alpha-linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega- and omega-1 positions. No activity is detected toward short-chain fatty acids (C10 to C14), cis-11-eicosenoic acid (C20:1), and C16 to C18 alkanes
-
-
?
additional information
?
-
-
isoform CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than alpha-linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega- and omega-1 positions. No activity is detected toward short-chain fatty acids (C10 to C14), cis-11-eicosenoic acid (C20:1), and C16 to C18 alkanes
-
-
?
additional information
?
-
isoform CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids
-
-
?
additional information
?
-
isoform CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids
-
-
?
additional information
?
-
isoform CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids
-
-
?
additional information
?
-
-
isoform CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids
-
-
?
additional information
?
-
isoform CYP52N1 shows minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid
-
-
?
additional information
?
-
isoform CYP52N1 shows minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid
-
-
?
additional information
?
-
isoform CYP52N1 shows minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid
-
-
?
additional information
?
-
-
isoform CYP52N1 shows minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid
-
-
?
additional information
?
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
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-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
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-
?
additional information
?
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52E3. Product identification und quantification by LC-MS and GC-MS. CYP52E3 displays activity in the resting cell system but not in the in vitro system. No formation of 17-hydroxy linoleic acid. No activity with stearic acid, linoleic acid, alpha-linolenic acid, cis-11-eicosenoic acid, arachidonic acid, hexadecane, octadecane, capric acid, and lauric acid
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52E3. Product identification und quantification by LC-MS and GC-MS. CYP52E3 displays activity in the resting cell system but not in the in vitro system. No formation of 17-hydroxy linoleic acid. No activity with stearic acid, linoleic acid, alpha-linolenic acid, cis-11-eicosenoic acid, arachidonic acid, hexadecane, octadecane, capric acid, and lauric acid
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52E3. Product identification und quantification by LC-MS and GC-MS. CYP52E3 displays activity in the resting cell system but not in the in vitro system. No formation of 17-hydroxy linoleic acid. No activity with stearic acid, linoleic acid, alpha-linolenic acid, cis-11-eicosenoic acid, arachidonic acid, hexadecane, octadecane, capric acid, and lauric acid
-
-
?
additional information
?
-
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52E3. Product identification und quantification by LC-MS and GC-MS. CYP52E3 displays activity in the resting cell system but not in the in vitro system. No formation of 17-hydroxy linoleic acid. No activity with stearic acid, linoleic acid, alpha-linolenic acid, cis-11-eicosenoic acid, arachidonic acid, hexadecane, octadecane, capric acid, and lauric acid
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52N1 Product identification und quantification by LC-MS and GC-MS. CYP52N1 displays activity in the resting cell system but not in the in vitro system. No activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52N1 Product identification und quantification by LC-MS and GC-MS. CYP52N1 displays activity in the resting cell system but not in the in vitro system. No activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52N1 Product identification und quantification by LC-MS and GC-MS. CYP52N1 displays activity in the resting cell system but not in the in vitro system. No activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid
-
-
?
additional information
?
-
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52N1 Product identification und quantification by LC-MS and GC-MS. CYP52N1 displays activity in the resting cell system but not in the in vitro system. No activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid
-
-
?
additional information
?
-
no activity with C10 to C12 fatty acids, myristic acid is a poor substrate, also no activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid. In coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52M1. Product identification und quantification by LC-MS and GC-MS
-
-
?
additional information
?
-
no activity with C10 to C12 fatty acids, myristic acid is a poor substrate, also no activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid. In coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52M1. Product identification und quantification by LC-MS and GC-MS
-
-
?
additional information
?
-
no activity with C10 to C12 fatty acids, myristic acid is a poor substrate, also no activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid. In coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52M1. Product identification und quantification by LC-MS and GC-MS
-
-
?
additional information
?
-
-
no activity with C10 to C12 fatty acids, myristic acid is a poor substrate, also no activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid. In coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52M1. Product identification und quantification by LC-MS and GC-MS
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
no activity with C10 to C12 fatty acids, myristic acid is a poor substrate, also no activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid. In coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52M1. Product identification und quantification by LC-MS and GC-MS
-
-
?
additional information
?
-
no activity with C10 to C12 fatty acids, myristic acid is a poor substrate, also no activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid. In coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52M1. Product identification und quantification by LC-MS and GC-MS
-
-
?
additional information
?
-
no activity with C10 to C12 fatty acids, myristic acid is a poor substrate, also no activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid. In coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52M1. Product identification und quantification by LC-MS and GC-MS
-
-
?
additional information
?
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52E3. Product identification und quantification by LC-MS and GC-MS. CYP52E3 displays activity in the resting cell system but not in the in vitro system. No formation of 17-hydroxy linoleic acid. No activity with stearic acid, linoleic acid, alpha-linolenic acid, cis-11-eicosenoic acid, arachidonic acid, hexadecane, octadecane, capric acid, and lauric acid
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52E3. Product identification und quantification by LC-MS and GC-MS. CYP52E3 displays activity in the resting cell system but not in the in vitro system. No formation of 17-hydroxy linoleic acid. No activity with stearic acid, linoleic acid, alpha-linolenic acid, cis-11-eicosenoic acid, arachidonic acid, hexadecane, octadecane, capric acid, and lauric acid
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52E3. Product identification und quantification by LC-MS and GC-MS. CYP52E3 displays activity in the resting cell system but not in the in vitro system. No formation of 17-hydroxy linoleic acid. No activity with stearic acid, linoleic acid, alpha-linolenic acid, cis-11-eicosenoic acid, arachidonic acid, hexadecane, octadecane, capric acid, and lauric acid
-
-
?
additional information
?
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52N1 Product identification und quantification by LC-MS and GC-MS. CYP52N1 displays activity in the resting cell system but not in the in vitro system. No activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52N1 Product identification und quantification by LC-MS and GC-MS. CYP52N1 displays activity in the resting cell system but not in the in vitro system. No activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid
-
-
?
additional information
?
-
in coassays with glucosyltransferase UGTA1, UGTA1 glycosylates all hydroxyl fatty acids generated by CYP52N1 Product identification und quantification by LC-MS and GC-MS. CYP52N1 displays activity in the resting cell system but not in the in vitro system. No activity with hexadecane, octadecane, capric acid, lauric acid, and cis-11-eicosenoic acid
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
lauric acid + [reduced NADPH-hemoprotein reductase] + O2 + H+
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
stearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
?
-
alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
low activity
-
-
?
alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
low activity
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
best substrate
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
best substrate
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
?
-
Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes
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?
additional information
?
-
substrate and product binding and release are much faster than overall rates of catalysis. Both the transfer of an electron to the ferrous-O2 complex and C-H bond-breaking limit the rate of P450 4A11 omega-oxidation
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?
additional information
?
-
-
substrate and product binding and release are much faster than overall rates of catalysis. Both the transfer of an electron to the ferrous-O2 complex and C-H bond-breaking limit the rate of P450 4A11 omega-oxidation
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-
?
additional information
?
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
-
enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
-
enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
?
-
enzyme CYP52M1 oxidizes C16 to C20 fatty acids preferentially. It converts oleic acid (C18:1) more efficiently than stearic acid (C18:0) and linoleic acid (C18:2) and much more effectively than linolenic acid (C18:3). No products are detected when C10 to C12 fatty acids are used as the substrates. CYP52M1 hydroxylates fatty acids at their omega and omega-1 positions. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
-
-
?
additional information
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enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
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additional information
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enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
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additional information
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enzyme CYP52E3 minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
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additional information
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enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
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additional information
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enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
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additional information
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enzyme CYP52N1 oxidizes C14 to C20 saturated and unsaturated fatty acids and preferentially oxidizes palmitic acid, oleic acid, and linoleic acid. It only catalyzes omega-hydroxylation of fatty acids. Transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 is much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1 in Starmerella bombicola
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Ascorbic Acid Deficiency
Ascorbic acid deficiency decreases the expression of CYP4A1 in liver microsomes of guinea pigs.
Carcinoma, Hepatocellular
Conjugated linoleic acid is a potent naturally occurring ligand and activator of PPARalpha.
Carcinoma, Hepatocellular
Cytochrome P450 4A11 expression in tumor cells: A favorable prognostic factor for hepatocellular carcinoma patients.
Carcinoma, Hepatocellular
The rat clofibrate-inducible CYP4A subfamily. II. cDNA sequence of IVA3, mapping of the Cyp4a locus to mouse chromosome 4, and coordinate and tissue-specific regulation of the CYP4A genes.
Cardiotoxicity
Chronic Doxorubicin Cardiotoxicity Modulates Cardiac Cytochrome P450-Mediated Arachidonic Acid Metabolism in Rats.
Endotoxemia
NS-398 reverses hypotension in endotoxemic rats: Contribution of eicosanoids, NO, and peroxynitrite.
Fatty Liver
Effects of binge ethanol on lipid homeostasis and oxidative stress in a rat model of nonalcoholic fatty liver disease.
Fatty Liver, Alcoholic
Undernutrition enhances alcohol-induced hepatocyte proliferation in the liver of rats fed via total enteral nutrition.
Glioma
Expression of CYP4A1 in U251 human glioma cell induces hyperproliferative phenotype in vitro and rapidly growing tumors in vivo.
Hepatomegaly
Hepatocellular hypertrophy and cell proliferation in Sprague-Dawley rats following dietary exposure to ammonium perfluorooctanoate occurs through increased activation of the xenosensor nuclear receptors PPAR? and CAR/PXR.
Hypercholesterolemia
Proteomic analysis for the impact of hypercholesterolemia on expressions of hepatic drug transporters and metabolizing enzymes.
Hyperlipidemias
Kaempferol Regulates the Lipid-Profile in High-Fat Diet-Fed Rats through an Increase in Hepatic PPAR? Levels.
Hyperlipidemias
Regulation of Obesity and Lipid Disorders by Extracts from Angelica acutiloba Root in High-fat Diet-induced Obese Rats.
Hypertension
20-Hydroxyeicosatetraenoic Acid (HETE)-dependent Hypertension in Human Cytochrome P450 (CYP) 4A11 Transgenic Mice: NORMALIZATION OF BLOOD PRESSURE BY SODIUM RESTRICTION, HYDROCHLOROTHIAZIDE, OR BLOCKADE OF THE TYPE 1 ANGIOTENSIN II RECEPTOR.
Hypertension
Arachidonate CYP hydroxylases of kidney contribute to formation of hypertension and maintenance of blood pressure.
Hypertension
CYP4A2-induced hypertension is 20-hydroxyeicosatetraenoic acid- and angiotensin II-dependent.
Hypertension
Effects of rosuvastatin correlated with the down-regulation of CYP4A1 in spontaneously hypertensive rats.
Hypertension
Endothelial dysfunction and hypertension in rats transduced with CYP4A2 adenovirus.
Hypertension
Endothelial-specific CYP4A2 overexpression leads to renal injury and hypertension via increased production of 20-HETE.
Hypertension
Fenofibrate Attenuates Hypertension in Goldblatt Hypertensive Rats: Role of 20-Hydroxyeicosatetraenoic Acid in the Nonclipped Kidney.
Hypertension
Induction of renal 20-hydroxyeicosatetraenoic acid by clofibrate attenuates high-fat diet-induced hypertension in rats.
Hypertension
Renal P450 metabolites of arachidonic acid and the development of hypertension in Dahl salt-sensitive rats.
Hypertension
Renal vascular cytochrome P450-derived eicosanoids in androgen-induced hypertension.
Hyperthyroidism
Regulation of CYP4A expression in rat by dehydroepiandrosterone and thyroid hormone.
Hypotension
A novel treatment strategy for sepsis and septic shock based on the interactions between prostanoids, nitric oxide, and 20-hydroxyeicosatetraenoic acid.
Hypotension
Arachidonate CYP hydroxylases of kidney contribute to formation of hypertension and maintenance of blood pressure.
Hypotension
Contribution of iNOS/sGC/PKG pathway, COX-2, CYP4A1, and gp91(phox) to the protective effect of 5,14-HEDGE, a 20-HETE mimetic, against vasodilation, hypotension, tachycardia, and inflammation in a rat model of septic shock.
Hypotension
Contribution of PPAR?/?/?, AP-1, importin-?3, and RXR? to the protective effect of 5,14-HEDGE, a 20-HETE mimetic, against hypotension, tachycardia, and inflammation in a rat model of septic shock.
Hypotension
Piroxicam Reverses Endotoxin-Induced Hypotension in Rats: Contribution of Vasoactive Eicosanoids and Nitric Oxide.
Infarction, Middle Cerebral Artery
Hyperbaric oxygenation and 20-HETE inhibition reduce stroke volume in female diabetic Sprague-Dawley rats.
Malnutrition
Undernutrition enhances alcohol-induced hepatocyte proliferation in the liver of rats fed via total enteral nutrition.
Neoplasms
Cytochrome P450 4A11 expression in tumor cells: A favorable prognostic factor for hepatocellular carcinoma patients.
Neoplasms
Expression of CYP4A1 in U251 human glioma cell induces hyperproliferative phenotype in vitro and rapidly growing tumors in vivo.
Neoplasms
Expression of xenobiotic-metabolizing enzymes by primary and secondary hepatic tumors in man.
Non-alcoholic Fatty Liver Disease
CYP4A11 is involved in the development of nonalcoholic fatty liver disease via ROS?induced lipid peroxidation and inflammation.
Obesity
Characterization of hepatic cytochrome P450 isozyme composition in the transgenic rat expressing low level human growth hormone.
Obesity
Regulation of Obesity and Lipid Disorders by Extracts from Angelica acutiloba Root in High-fat Diet-induced Obese Rats.
Sepsis
Differential expression of cytochrome P450 isoforms in the lungs of septic animals.
Shock, Septic
A novel treatment strategy for sepsis and septic shock based on the interactions between prostanoids, nitric oxide, and 20-hydroxyeicosatetraenoic acid.
Shock, Septic
Contribution of iNOS/sGC/PKG pathway, COX-2, CYP4A1, and gp91(phox) to the protective effect of 5,14-HEDGE, a 20-HETE mimetic, against vasodilation, hypotension, tachycardia, and inflammation in a rat model of septic shock.
Shock, Septic
Contribution of PPAR?/?/?, AP-1, importin-?3, and RXR? to the protective effect of 5,14-HEDGE, a 20-HETE mimetic, against hypotension, tachycardia, and inflammation in a rat model of septic shock.
Tachycardia
Contribution of iNOS/sGC/PKG pathway, COX-2, CYP4A1, and gp91(phox) to the protective effect of 5,14-HEDGE, a 20-HETE mimetic, against vasodilation, hypotension, tachycardia, and inflammation in a rat model of septic shock.
Tachycardia
Contribution of PPAR?/?/?, AP-1, importin-?3, and RXR? to the protective effect of 5,14-HEDGE, a 20-HETE mimetic, against hypotension, tachycardia, and inflammation in a rat model of septic shock.
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Hoch, U.; Zhang, Z.; Kroetz, D.L.; Ortiz de Montellano, P.R.
Structural determination of the substrate specificities and regioselectivities of the rat and human fatty acid omega-hydroxylases
Arch. Biochem. Biophys.
373
63-71
2000
Rattus norvegicus (P08516), Rattus norvegicus (P20816), Rattus norvegicus (P20817), Rattus norvegicus (P24464), Homo sapiens (Q02928), Homo sapiens
brenda
Benveniste, I.; Saito, T.; Wang, Y.; Kandel, S.; Huang, H.; Pinot, F.; Kahn, R.A.; Salauen, J.; Shimoji, M.
Evolutionary relationship and substrate specificity of Arabidopsis thaliana fatty acid omega-hydroxylase
Plant Sci.
170
326-338
2006
Arabidopsis thaliana (Q9ZUX1)
brenda
Nakano, M.; Kelly, E.J.; Rettie, A.E.
Expression and characterization of CYP4V2 as a fatty acid omega-hydroxylase
Drug Metab. Dispos.
37
2119-2122
2009
Homo sapiens
brenda
Dobritsa, A.A.; Shrestha, J.; Morant, M.; Pinot, F.; Matsuno, M.; Swanson, R.; Moller, B.L.; Preuss, D.
CYP704B1 is a long-chain fatty acid omega-hydroxylase essential for sporopollenin synthesis in pollen of Arabidopsis
Plant Physiol.
151
574-589
2009
Arabidopsis thaliana (Q9C788)
brenda
Huang, F.C.; Peter, A.; Schwab, W.
Expression and characterization of CYP52 genes involved in the biosynthesis of sophorolipid and alkane metabolism from Starmerella bombicola
Appl. Environ. Microbiol.
80
766-776
2014
Starmerella bombicola (B8QHP1), Starmerella bombicola (B8QHP3), Starmerella bombicola (B8QHP5), Starmerella bombicola
brenda
Benveniste, I.; Tijet, N.; Adas, F.; Philipps, G.; Salan, J.; Durst, F.
CYP86A1 from Arabidopsis thaliana encodes a cytochrome P450-dependent fatty acid omega-hydroxylase
Biochem. Biophys. Res. Commun.
243
688-693
1998
Arabidopsis thaliana (P48422)
brenda
Van Bogaert, I.N.; De Mey, M.; Demey, M.; Develter, D.; Soetaert, W.; Vandamme, E.J.
Importance of the cytochrome P450 monooxygenase CYP52 family for the sophorolipid-producing yeast Candida bombicola
FEMS Yeast Res.
9
87-94
2009
Starmerella bombicola (B8QHP1), Starmerella bombicola
brenda
Kawashima, H.; Kusunose, E.; Kikuta, Y.; Kinoshita, H.; Tanaka, S.; Yamamoto, S.; Kishimoto, T.; Kusunose, M.
Purification and cDNA cloning of human liver CYP4A fatty acid omega-hydroxylase
J. Biochem.
116
74-80
1994
Homo sapiens (Q02928)
brenda
Hiratsuka, M.; Matsuura, T.; Watanabe, E.; Sato, M.; Suzuki, Y.
Sex and strain differences in constitutive expression of fatty acid omega-hydroxylase (CYP4A-related proteins) in mice
J. Biochem.
119
340-345
1996
Mus musculus
brenda
Gatica, A.; Aguilera, M.C.; Contador, D.; Loyola, G.; Pinto, C.O.; Amigo, L.; Tichauer, J.E.; Zanlungo, S.; Bronfman, M.
P450 CYP2C epoxygenase and CYP4A omega-hydroxylase mediate ciprofibrate-induced PPARalpha-dependent peroxisomal proliferation
J. Lipid Res.
48
924-934
2007
Rattus norvegicus
brenda
Duan, H.; Schuler, M.A.
Differential expression and evolution of the Arabidopsis CYP86A subfamily
Plant Physiol.
137
1067-1081
2005
Arabidopsis thaliana (O23066), Arabidopsis thaliana (O80823), Arabidopsis thaliana (P48422), Arabidopsis thaliana (Q9CAD6), Arabidopsis thaliana (Q9LMM1)
brenda
Huang, F.; Peter, A.; Schwab, W.
Expression and characterization of CYP52 genes involved in the biosynthesis of sophorolipid and alkane metabolism from Starmerella bombicola
Appl. Environ. Microbiol.
80
766-776
2014
Starmerella bombicola (B8QHP1), Starmerella bombicola (B8QHP3), Starmerella bombicola (B8QHP5), Starmerella bombicola, Starmerella bombicola ATCC 22214 (B8QHP1), Starmerella bombicola ATCC 22214 (B8QHP3), Starmerella bombicola ATCC 22214 (B8QHP5)
brenda
Kim, D.; Cha, G.S.; Nagy, L.D.; Yun, C.H.; Guengerich, F.P.
Kinetic analysis of lauric acid hydroxylation by human cytochrome P450 4A11
Biochemistry
53
6161-6172
2014
Homo sapiens (Q02928), Homo sapiens
brenda
Saito, T.; Honda, M.; Takahashi, M.; Tsukada, C.; Ito, M.; Katono, Y.; Hosono, H.; Saigusa, D.; Suzuki, N.; Tomioka, Y.; Hirasawa, N.; Hiratsuka, M.
Functional characterization of 10 CYP4A11 allelic variants to evaluate the effect of genotype on arachidonic acid omega-hydroxylation
Drug Metab. Pharmacokinet.
30
119-122
2015
Homo sapiens (Q02928)
brenda
Han, S.; Cha, G.S.; Chun, Y.J.; Lee, C.H.; Kim, D.; Yun, C.H.
Biochemical analysis of recombinant CYP4A11 allelic variant enzymes W126R, K276T and S353G
Drug Metab. Pharmacokinet.
31
445-450
2016
Homo sapiens (Q02928)
brenda
Bjelica, A.; Haggitt, M.L.; Woolfson, K.N.; Lee, D.P.; Makhzoum, A.B.; Bernards, M.A.
Fatty acid omega-hydroxylases from Solanum tuberosum
Plant Cell Rep.
35
2435-2448
2016
Solanum tuberosum (B9TST1), Solanum tuberosum
brenda
Zhang, X.; Li, S.; Zhou, Y.; Su, W.; Ruan, X.; Wang, B.; Zheng, F.; Warner, M.; Gustafsson, J.; Guan, Y.
Ablation of cytochrome P450 omega-hydroxylase 4A14 gene attenuates hepatic steatosis and fibrosis
Proc. Natl. Acad. Sci. USA
114
3181-3185
2017
Mus musculus (O35728)
brenda
Uehara, S.; Uno, Y.; Ishii, S.; Inoue, T.; Sasaki, E.; Yamazaki, H.
Marmoset cytochrome P450 4A11, a novel arachidonic acid and lauric acid omega-hydroxylase expressed in liver and kidney tissues
Xenobiotica
47
553-561
2017
Callithrix jacchus (A0A1P8NQJ7)
brenda