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9,10-epoxystearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxy-9,10-epoxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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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
Substrates: -
Products: -
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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
Substrates: -
Products: -
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isolauric acid + [reduced NADPH-hemoprotein reductase] + O2
11-hydroxyisolauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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isomyristic acid + [reduced NADPH-hemoprotein reductase] + O2
13-hydroxyisomyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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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
Substrates: -
Products: -
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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
Substrates: best substrate
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
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Substrates: CYP4V2 is a selective omega-hydroxylase of saturated, medium-chain fatty acids with relatively high catalytic efficiency toward myristic acid
Products: -
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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
Substrates: -
Products: -
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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
Substrates: -
Products: -
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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
Substrates: -
Products: -
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tridecanoic acid + [reduced NADPH-hemoprotein reductase] + O2
13-hydroxytridecanoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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undecanoic acid + [reduced NADPH-hemoprotein reductase] + O2
11-hydroxyundecanoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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additional information
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alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: low activity
Products: -
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alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: low activity
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 2.4:1
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 2:1
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 6:1
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 16% of the activity with palmitic acid
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 28% yield
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: substrate for isoforms CYP86A1, CYP86A2, CYP86A4, CYP86A7, CYP86A8
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
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Substrates: -
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 2.5:1
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 2.5:1
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 3:1
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 40:1
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 6:1
Products: -
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linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 52% of the activity with palmitic acid
Products: -
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linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 28% yield
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 49% of the activity with palmitic acid
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 1.6:1
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 1.2:1
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 1.6:1
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 3:1
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 28% yield
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 61% of the activity with palmitic acid
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: best substrate
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: best substrate
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 21% yield
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 28% yield
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 1.6:1
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 1.6:1
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: regioselectivity of omega:omega-1 hydroxylation is 1:1
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 44% yield
Products: -
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palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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additional information
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Substrates: isoform CYP86A1 catalyze the omega-hydroxylation of saturated and unsaturated fatty acids with chain lengths from C12 to C18 but not of hexadecane
Products: -
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additional information
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Substrates: no substrate palmitoyl-CoA
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additional information
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Substrates: no substrate: 12-hydroxylauric acid, lauric acid, cinnamate, p-coumarate, ferulate, sinapate, and p-coumaroyl shikimate
Products: -
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additional information
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Substrates: 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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Substrates: 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
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additional information
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Substrates: octanoic acid is not detectably omega-hydroxylated by CYP4V2
Products: -
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additional information
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Substrates: isoform CYP4A11 catalyzes the omega- and omega-1-hydroxylation of various fatty acids
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additional information
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Substrates: 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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Substrates: 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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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: isoform CYP52N1 shows minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid
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additional information
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Substrates: isoform CYP52N1 shows minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid
Products: -
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additional information
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Substrates: isoform CYP52N1 shows minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid
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additional information
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Substrates: isoform CYP52N1 shows minor omega-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid
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additional information
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
?
-
-
Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
-
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
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additional information
?
-
Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
?
additional information
?
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Substrates: 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
Products: -
?
additional information
?
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Substrates: 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
Products: -
?
additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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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
Substrates: -
Products: -
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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
Substrates: -
Products: -
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palmitoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxypalmitoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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stearic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxystearic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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additional information
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-
alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: low activity
Products: -
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alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinolenic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: low activity
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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linoleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxylinoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: best substrate
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: best substrate
Products: -
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oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
?
additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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 CYP5