EC Number   |
General Information |
Reference |
|---|
   1.3.1.124 | malfunction |
cold intolerance of Decr-/- mice is due to failure in maintaining appropriate heat production at least partly due to failure of brown adipose tissue (BAT) thermogenesis |
760176 |
| 1.3.1.124 | malfunction |
enzyme (DECR1) knockout induces ER stress and sensitises castration-resistant prostate cancer cells to ferroptosis. In vivo, DECR1 deletion impairs lipid metabolism and reduces tumour growth of castration-resistant prostate cancer, emphasizing the importance of DECR1 in the development of treatment resistance |
759825 |
| 1.3.1.124 | metabolism |
key enzyme required for beta-oxidation of polyunsaturated fatty acids |
760176 |
| 1.3.1.124 | physiological function |
an SPS19 deleted strain is unable to utilize petroselineate (cis-C18:1(6)) as the sole carbon source, but remains viable on oleate (cis-C18:1(9)). SPS19 is dispensable for growth and sporulation on solid acetate and oleate media, but is essential for these processes to occur on petroselineate |
759455 |
| 1.3.1.124 | physiological function |
cold intolerance of Decr?/? mice is due to failure in maintaining appropriate heat production at least partly due to failure of brown adipose tissue thermogenesis. Activation of lipolysis is attenuated despite of functional norepinephrine-signaling and inappropriate expression of genes contributing to thermogenesis in interscapular brown adipose rissue when the Decr?/? mice are exposed to cold |
760176 |
| 1.3.1.124 | physiological function |
DECR1 participates in redox homeostasis by controlling the balance between saturated and unsaturated phospholipids. DECR1 knockout induces ER stress and sensitizes castration-resistant prostate cancer cells to ferroptosis. In vivo, DECR1 deletion impairs lipid metabolism and reduces castration-resistant prostate cancer tumor growth |
759825 |
| 1.3.1.124 | physiological function |
dienoyl-CoA and NADPH bind to the 2,4-dienoyl-CoA reductase via a sequential kinetic mechanism with a random order of nucleotide and dienoyl-CoA addition. A proton transfer step is rate limiting for (2E,4E)-hexa-2,4-dienoyl-CoA substrate, addition of a phenyl ring to the diene in 5-phenyl-(2E,4E)-2,4-pentadienoyl-CoA results in the reversal of the rate-determining step. The chemical mechanism is stepwise where hydride transfer from NADPH occurs followed by protonation of the dienolate intermediate |
758774 |
| 1.3.1.124 | physiological function |
human mitochondrial 2,4-reductase functions in the beta-oxidation of unsaturated fatty acids. A yeast sps19D mutant expressing human 2,4-reductase ending with the native C-terminus cannot grow on petroselinic acid medium but can grow when the protein is extended with a peroxisomal targeting tripeptide, Ser-Lys-Leu |
758746 |
| 1.3.1.124 | physiological function |
in vitro, 4-cis-decenoyl-CoA is only degraded when the 2,4-dienoyl-CoA reductase step in linoleic acid degradation is not blocked by lack of NADPH |
759449 |
| 1.3.1.124 | physiological function |
metabolism of unsaturated fatty acids occurs mainly in the mitochondria and the peroxisomes of the proximal tubule in the kidney |
759324 |
