EC |
1.14.19.24 |
Accepted name: |
acyl-CoA 11-(E)-desaturase |
Reaction: |
an acyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = an (11E)-enoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
Systematic name: |
acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (11,12 trans-dehydrogenating) |
Comments: |
Involved in sex pheromone synthesis in the Lepidoptera (moths). The enzyme from the moth Spodoptera littoralis prefers 13:0 and 14:0 substrates. The product is formed by the stereospecific removal of the pro-R H at C-11 and the pro-S H at C-12. cf. EC 1.14.19.5, acyl-CoA 11-(Z)-desaturase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 199543-17-4 |
References: |
1. |
Foster, S. P. and Roelofs, W. L. Biosynthesis of a monoene and a conjugated diene sex pheromone component of the lightbrown apple moth by 11 desaturation. Experientia 46 (1990) 269–273. |
2. |
Martinez, T., Fabrias, G. and Camps, F. Sex pheromone biosynthetic pathway in Spodoptera littoralis and its activation by a neurohormone. J. Biol. Chem. 265 (1990) 1381–1387. [PMID: 2295634] |
3. |
Navarro, I., Font, I., Fabrias, G. and Camps, F. Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in the biosynthesis of Spodoptera littoralis sex pheromone. J. Am. Chem. Soc. 119 (1997) 11335–11336. |
4. |
Pinilla, A., Camps, F. and Fabrias, G. Cryptoregiochemistry of the Δ11-myristoyl-CoA desaturase involved in the biosynthesis of Spodoptera littoralis sex pheromone. Biochemistry 38 (1999) 15272–15277. [DOI] [PMID: 10563812] |
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[EC 1.14.19.24 created 2000 as EC 1.14.99.31, transferred 2015 to EC 1.14.19.24] |
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