EC Number   |
Reaction |
Reference |
|---|
    1.14.19.1 | stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. Formerly EC 1.14.99.5 |
- |
| 1.14.19.1 | stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
arginyl and tyrosyl residues expected in the active site of enzyme |
- |
| 1.14.19.1 | stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
cold exposure leads to an induced activity, in vivo cooling causes an activity induction of up to 15 to 30fold. Increase of desaturase synthesis by means of activated gene transcription. Transfer of cells to 10°C causes a smaller increase in activity compared to cells maintained at 30°C |
-, 437669 |
| 1.14.19.1 | stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
cytochrome b5, cytochrome b5 reductase and lipid and/or detergent are needed for all assays. A cis-hydrogen abstraction mechanism is involved in desaturation |
-, 437648 |
| 1.14.19.1 | stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
electron flow from NADH to cytochrome b5, via cytochrome b5 reductase. Different types of acyl-CoA desaturation show immunological differences |
437649 |
| 1.14.19.1 | stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
existence of three highly homologous isoforms: SCD1, SCD2 and SCD3 which show different substrate specificities, here SCD1 is mainly analysed |
437671 |
| 1.14.19.1 | stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
incorporation of fatty acid into phospholipid. Enzyme may contain an essential thiol group. Endogenous saturated phospholipid is desaturated rapidly in all experiments in contrast with exogenous saturated phospholipid, which generally is not desaturated |
437650 |
| 1.14.19.1 | stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
increase of activity induced by cold is preceded by the activation of latent desaturase, probably by a posttranslational mechanism. Amounts of desaturase transcript are increased as a result of cold-induced gene transcription |
437668 |
| 1.14.19.1 | stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
introduction of double bond at position 9 |
437658 |
| 1.14.19.1 | stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
introduction of double bonds at fixed positions from the carboxyl group of the fatty acid. D-hydrogen atoms are removed during desaturation. Mixed-function oxidase, acting via hydroxy acid intermediates. Acetyl-CoA desaturase, carboxylase and fatty acid synthetase are all controlled together as a unit and influenced by dietary components |
437657 |
