EC Number   |
Natural Substrates |
|---|
   1.6.2.2 | 2 ferricytochrome b5 + NADH |
- |
| 1.6.2.2 | 2 ferricytochrome b5 + NADH |
membrane bound form of somatic cells: essential for lipid metabolism |
| 1.6.2.2 | 2 ferricytochrome b5 + NADH |
involved in desaturation of fatty acids |
| 1.6.2.2 | 2 ferricytochrome b5 + NADH |
involved in metabolism of endogenous compounds such as steroids, drugs, carcinogens, environmental pollutants |
| 1.6.2.2 | 2 ferricytochrome b5 + NADH |
enzyme is assumed to be part of an endoplasmic reticulum associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 to endoplasmic reticulum associated fatty acyl desaturase and related hydroxylases as in mammals |
| 1.6.2.2 | 2 ferricytochrome b5 + NADH |
enzyme complex drives the entire sterol 14-demethylation reaction |
| 1.6.2.2 | 2 ferricytochrome b5 + NADH |
enzyme participates in methemoglobin reduction in erythrocytes, in other tissues it plays a role in elongation and desaturation of fatty acids, P-450 mediated drug metabolism and cholesterol biosynthesis as part of the microsomal electron transfer system |
| 1.6.2.2 | 2 ferricytochrome b5 + NADH |
soluble form of erythrocytes: reduction of methemoglobin |
| 1.6.2.2 | 2 ferricytochrome b5 + NADH |
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics |
| 1.6.2.2 | 2 ferricytochrome b5 + NADH |
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, enzyme defects causes methemoglobinemia type I or type II |
