1.14.14.80: long-chain fatty acid omega-monooxygenase
This is an abbreviated version!
For detailed information about long-chain fatty acid omega-monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.80
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1.14.14.80
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peroxisome
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arachidonic
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20-hete
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lauric
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20-hydroxyeicosatetraenoic
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clofibrate
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omega-hydroxylase
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cyp2c11
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omega-hydroxylation
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proliferators
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cyp3a1
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pparalpha
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epoxyeicosatrienoic
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ethoxyresorufin
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cyp2j3
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ja-ile
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sporopollenin
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interlobar
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cyp94b3
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clofibrate-inducible
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omega-1
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ciprofibrate
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medicine
- 1.14.14.80
- peroxisome
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arachidonic
- 20-hete
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lauric
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20-hydroxyeicosatetraenoic
- clofibrate
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omega-hydroxylase
- cyp2c11
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omega-hydroxylation
- proliferators
- cyp3a1
- pparalpha
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epoxyeicosatrienoic
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ethoxyresorufin
- cyp2j3
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ja-ile
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sporopollenin
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interlobar
- cyp94b3
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clofibrate-inducible
- omega-1
- ciprofibrate
- medicine
Reaction
Synonyms
At1g69500, At2g27690, CYP4A, CYP4A1, CYP4A11, CYP4A14, CYP4A2, CYP4A3, CYP4A8, CYP4V2, CYP52-E3, CYP52-M1, CYP52-N1, CYP52E3, CYP52M1, CYP52N1, CYP704B1, CYP86A, CYP86A1, CYP86A33, CYP94C1, cytochrome P450 4A11, cytochrome P450 704B1, cytochrome P450 86A1, EC 1.14.13.205, Fatty acid omega-hydroxylase, Lauric acid omega-hydroxylase, omega-hydroxylase, P450 4A11
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Natural Substrates Products
Natural Substrates Products on EC 1.14.14.80 - long-chain fatty acid omega-monooxygenase
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REACTION DIAGRAM
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
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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
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palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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stearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
low activity
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alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
low activity
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20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
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18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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?
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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?
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
best substrate
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
best substrate
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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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
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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
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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
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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 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 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
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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
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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
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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
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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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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 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
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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
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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
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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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