Bombykol

Bombykol is a pheromone released by the female silkworm moth to attract mates. It is also the sex pheromone in the wild silk moth (Bombyx mandarina).^[1][2] Discovered by Adolf Butenandt in 1959, it was the first pheromone to be characterized chemically.^[3]

Bombykol

Names
Preferred IUPAC name (10E,12Z)-Hexadeca-10,12-dien-1-ol
Identifiers
CAS Number	765-17-3 Y
3D model (JSmol)	Interactive image Interactive image
ChEBI	CHEBI:41200 Y
ChemSpider	392860 Y
PubChem CID	445128
UNII	LZT8R8TVZ7 Y
CompTox Dashboard (EPA)	DTXSID00894769
InChI InChI=1S/C16H30O/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17/h4-7,17H,2-3,8-16H2,1H3/b5-4-,7-6+ Y Key: CIVIWCVVOFNUST-SCFJQAPRSA-N Y InChI=1/C16H30O/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17/h4-7,17H,2-3,8-16H2,1H3/b5-4-,7-6+ Key: CIVIWCVVOFNUST-SCFJQAPRBG
SMILES CCC/C=C\C=C\CCCCCCCCCO OCCCCCCCCC\C=C\C=C/CCC
Properties
Chemical formula	C16H30O
Molar mass	238.415 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Y verify (what is YN ?) Infobox references

Biosynthesis of bombykol starting from palmitoyl-CoA

Minute quantities of this pheromone can be used per acre of land to confuse male insects about the location of their female partners. It can thus serve as a lure in traps to remove insects effectively without spraying crops with large amounts of pesticides. Butenandt named the substance after the moth's Latin name Bombyx mori.^[4]

In vivo it appears that bombykol is the natural ligand for a pheromone binding protein, BmorPBP, which escorts the pheromone to the pheromone receptor.^[5]

Biosynthesis

Bombykol is known to be derived from acetyl-CoA via the C-16 fatty acyl palmitoyl-CoA.^[6] Palmitoyl-CoA is converted to bombykol in steps that involve desaturation and reductive modification of the carbonyl carbon.^[7] Compared to other Type I pheromones, bombykol biosynthesis does not need chain-shortening or any other kind of modification of the terminal hydroxyl group.

A desaturase enzyme encoded by the gene Bmpgdesat1 (Desat1), produces the monoene (11Z)-hexadecenoyl-CoA as well as the diene (10E,12Z)-10,12-hexadecadienoyl-CoA. This desaturase is the only enzyme necessary to catalyze these two consecutive desaturation steps.^[8]

The bombykol acyl precursor (10E,12Z)-10,12-hexadecadienoate is primarily found as a triacylglycerol ester in the cytoplasmic lipid droplets of pheromone gland cells of the moth. And when the adult females emerge from their pupae, the neurohormone PBAN (pheromone biosynthesis-activating neuropeptide) start signaling events that help control the lipolysis of the stored triacylglycerols, releasing (10E,12Z)-10,12-hexadecadienoate for its final reductive modification.^[9][10][11] The mechanism of the lipolytic release of (10E,12Z)-10,12-hexadecadienoate from triacylglycerols is not completely known but the candidate lipase-encoding genes have been identified.^[9][10]