A fatty acyl-CoA reductase highly expressed in the head of honey bee (Apis mellifera) involves biosynthesis of a wide range of aliphatic fatty alcohols

Insect Biochem Mol Biol. 2010 Sep;40(9):641-9. doi: 10.1016/j.ibmb.2010.06.004. Epub 2010 Jun 11.

Abstract

Honey bees (Apis mellifera) are social insects which have remarkable complexity in communication pheromones. These chemical signals comprise a mixture of hydrocarbons, wax esters, fatty acids, aldehydes and alcohols. In this study, we detected several long chain aliphatic alcohols ranging from C18-C32 in honey bees and the level of these alcohols varied in each body segment. C18:0Alc and C20:0Alc are more pronounced in the head, whereas C22:0Alc to C32Alc are abundant in the abdomen. One of the cDNAs coding for a fatty acyl-CoA reductase (AmFAR1) involved in the synthesis of fatty alcohols was isolated and characterized. AmFAR1 was ubiquitously expressed in all body segments with the predominance in the head of honey bees. Heterologous expression of AmFAR1 in yeast revealed that AmFAR1 could convert a wide range of fatty acids (14:0-22:0) to their corresponding alcohols, with stearic acid 18:0 as the most preferred substrate. The substrate preference and the expression pattern of AmFAR1 were correlated with the level of total fatty alcohols in bees. Reconstitution of the wax biosynthetic pathway by heterologous expression of AmFAR1, together with Euglena wax synthase led to the high level production of medium to long chain wax monoesters in yeast.

MeSH terms

  • Aldehyde Oxidoreductases / chemistry
  • Aldehyde Oxidoreductases / metabolism*
  • Animals
  • Bees / enzymology*
  • Bees / metabolism
  • Fatty Alcohols / chemistry
  • Fatty Alcohols / metabolism*
  • Head
  • Insect Proteins / chemistry
  • Insect Proteins / metabolism*
  • Phylogeny
  • Sequence Alignment
  • Sequence Analysis, Protein

Substances

  • Fatty Alcohols
  • Insect Proteins
  • Aldehyde Oxidoreductases
  • hexadecanal dehydrogenase (acylating)