Stearoyl-CoA 9-desaturase

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In enzymology, a stearoyl-CoA 9-desaturase (EC 1.14.19.1) is an enzyme that catalyzes the chemical reaction

stearoyl-CoA + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ $\rightleftharpoons$ oleoyl-CoA + 2 ferricytochrome b₅ + 2 H₂O

The 4 substrates of this enzyme are stearoyl-CoA, ferrocytochrome b5, O₂, and H⁺, whereas its 3 products are oleoyl-CoA, ferricytochrome b5, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with oxidation of a pair of donors resulting in the reduction of O to two molecules of water. The systematic name of this enzyme class is stearoyl-CoA,ferrocytochrome-b5:oxygen oxidoreductase (9,10-dehydrogenating). Other names in common use include Delta9-desaturase, acyl-CoA desaturase, fatty acid desaturase, and stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase. This enzyme participates in polyunsaturated fatty acid biosynthesis and ppar signaling pathway. It employs one cofactor, iron.

[edit] References

IUBMB entry for 1.14.19.1
BRENDA references for 1.14.19.1 (Recommended.)
PubMed references for 1.14.19.1
PubMed Central references for 1.14.19.1
Google Scholar references for 1.14.19.1
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Oshino N, Imai Y, Sato R (1966). "Electron-transfer mechanism associated with fatty acid desaturation catalyzed by liver microsomes". Biochim. Biophys. Acta. 128: 13–27. PMID 4382040.
Oshino N, Imai Y, Sato R (Tokyo). "A function of cytochrome b5 in fatty acid desaturation by rat liver microsomes". J. Biochem.: 155–67. PMID 5543646.
Strittmatter P, Spatz L, Corcoran D, Rogers MJ, Setlow B, Redline R (1974). "Purification and properties of rat liver microsomal stearyl coenzyme A desaturase". Proc. Natl. Acad. Sci. U. S. A. 71: 4565–9. doi:10.1073/pnas.71.11.4565. PMID 4373719.