| EC |
1.14.19.1 |
| Accepted name: |
stearoyl-CoA 9-desaturase |
| Reaction: |
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
| Other name(s): |
Δ9-desaturase; acyl-CoA desaturase; fatty acid desaturase; stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase |
| Systematic name: |
stearoyl-CoA,ferrocytochrome-b5:oxygen oxidoreductase (9,10-dehydrogenating) |
| Comments: |
An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2). |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9014-34-0 |
| References: |
| 1. |
Fulco, A.J. and Bloch, K. Cofactor requirements for the formation of Δ9-unsaturated fatty acids in Mycobacterium phlei. J. Biol. Chem. 239 (1964) 993–997. [PMID: 14167617] |
| 2. |
Oshino, N., Imai, Y. and Sato, R. Electron-transfer mechanism associated with fatty acid desaturation catalyzed by liver microsomes. Biochim. Biophys. Acta 128 (1966) 13–27. [PMID: 4382040] |
| 3. |
Oshino, N., Imai, Y. and Sato, R. A function of cytochrome b5 in fatty acid desaturation by rat liver microsomes. J. Biochem. (Tokyo) 69 (1971) 155–167. [PMID: 5543646] |
| 4. |
Strittmatter, P., Sputz, L., Corcoran, D., Rogers, M.J., Setlow, B. and Redline, R. Purification and properties of rat liver microsomal stearyl coenzyme A desaturase. Proc. Natl. Acad. Sci. USA 71 (1974) 4565–4569. [DOI] [PMID: 4373719] |
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| [EC 1.14.19.1 created 1972 as EC 1.14.99.5, modified 1986, modified 2000, transferred 2000 to EC 1.14.19.1, modified 2003] |
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