EC 1 - Oxidoreductases
EC 1.14 - Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O2
EC 1.14.19 - With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
EC 1.14.19.1 - Stearoyl-CoA 9-desaturase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.14.19.1
Names
Accepted name:
stearoyl-CoA 9-desaturase
Other
names:
Δ9-desaturase
acyl-CoA desaturase
fatty acid desaturase
stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase
stearoyl-CoA desaturase
acyl-CoA desaturase
fatty acid desaturase
stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase
stearoyl-CoA desaturase
Systematic name:
stearoyl-CoA,ferrocytochrome-b5:oxygen oxidoreductase (9,10-dehydrogenating)
Reaction
- stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Cofactor
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
Protein domains and families:
PROSITE:PDOC00399
Gene Ontology:
GO:0004768
CAS Registry Number:
9014-34-0
References
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Cofactor requirements for the formation of Δ9-unsaturated fatty acids in Mycobacterium phlei.J. Biol. Chem. 239 : 993-997 (1964). [PMID: 14167617]
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Electron-transfer mechanism associated with fatty acid desaturation catalyzed by liver microsomes.Biochim. Biophys. Acta 128 : 13-27 (1966). [PMID: 4382040]
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A function of cytochrome b5 in fatty acid desaturation by rat liver microsomes.J. Biochem. (Tokyo) 69 : 155-167 (1971). [PMID: 5543646]
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Purification and properties of rat liver microsomal stearyl coenzyme A desaturase.Proc. Natl. Acad. Sci. USA 71 : 4565-4569 (1974). [PMID: 4373719]
[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]