Aldehyde reductase activity in the antennae of Helicoverpa armigera.
Insect Mol Biol
; 23(3): 330-40, 2014 Jun.
Article
em En
| MEDLINE
| ID: mdl-24580848
ABSTRACT
In the present study, we identified two aldehyde reductase activities in the antennae of Helicoverpa species, NADH and NADPH-dependent activity. We expressed one of these proteins of H. armigera, aldo-keto reductase (AKR), which bears 56% identity to bovine aldose reductase, displays a NADPH-dependent activity and is mainly expressed in the antennae of adults. Whole-mount immunostaining showed that the enzyme is concentrated in the cells at the base of chemosensilla and in the nerves. The enzyme activity of H. armigeraâ
AKR is markedly different from those of mammalian enzymes. The best substrates are linear aliphatic aldehydes of 8-10 carbon atoms, but not hydroxyaldehydes. Both pheromone components of H. armigera, which are unsaturated aldehydes of 16 carbons, are very poor substrates. Unlike mammalian AKRs, the H. armigera enzyme is weakly affected by common inhibitors and exhibits a different behaviour from the action of thiols. A model of the enzyme suggests that the four cysteines are in their reduced form, as are the seven cysteines of mammalian enzymes. The occurrence of orthologous proteins in other insect species, that do not use aldehydes as pheromones, excludes the possibility of classifying this enzyme among the pheromone-degrading enzymes, as has been previously described in other insect species.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Temas:
Geral
Base de dados:
MEDLINE
Assunto principal:
Antenas de Artrópodes
/
Mariposas
Limite:
Animals
Idioma:
En
Revista:
Insect Mol Biol
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
China