Pen_1990_Genetica_81_125

Reference

Title : Serine esterases: structural conservation during animal evolution and variability in enzymatic properties in the genus Drosophila - Pen_1990_Genetica_81_125
Author(s) : Pen J , Bolks GJ , Hoeksema-Du Pui ML , Beintema JJ
Ref : Genetica , 81 :125 , 1990
Abstract :

Both general esterases and acetylcholinesterases have been shown to be members of a homologous superfamily of serine esterases. A comparison of N-terminal sequences demonstrates that esterase-4 and -5 from Drosophila mojavensis belong to this family as well, with esterase-6 and esterase-P from D. melanogaster being the closest relatives. In order to investigate the presence of immunologically related esterases in other Drosophila species, crude larval extracts from five species were applied to two immunoaffinity columns with antibodies directed against esterase-4 and esterase-5 from D. mojavensis. The substrate preference for either 1- or 2-naphthyl acetate was determined. Both esterase-4 and esterase-5 from D. mojavensis are 'normally' specific for 2-naphthyl esters, but at least three of the cross-reacting esterases from the other species have a preference for 1-naphthyl esters. This difference in substrate preference is another example of the variability observed with Drosophila esterases.

PubMedSearch : Pen_1990_Genetica_81_125
PubMedID: 2124571

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Citations formats

Pen J, Bolks GJ, Hoeksema-Du Pui ML, Beintema JJ (1990)
Serine esterases: structural conservation during animal evolution and variability in enzymatic properties in the genus Drosophila
Genetica 81 :125

Pen J, Bolks GJ, Hoeksema-Du Pui ML, Beintema JJ (1990)
Genetica 81 :125