IUBMB Enzyme Nomenclature

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:

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. [PMID: 10563812]

[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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