EC Number   |
Natural Substrates |
|---|
   1.14.14.80 | alpha-linolenic acid + [reduced NADPH-hemoprotein reductase] + O2 |
low activity |
| 1.14.14.80 | arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2 |
- |
| 1.14.14.80 | lauric acid + [reduced NADPH-hemoprotein reductase] + O2 |
- |
| 1.14.14.80 | lauric acid + [reduced NADPH-hemoprotein reductase] + O2 + H+ |
- |
| 1.14.14.80 | linoleic acid + [reduced NADPH-hemoprotein reductase] + O2 |
- |
| 1.14.14.80 | more |
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 |
| 1.14.14.80 | more |
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 |
| 1.14.14.80 | more |
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 |
| 1.14.14.80 | more |
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 |
| 1.14.14.80 | more |
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 |
