Esterase-6 allozymes: biochemical studies of two common and one rare variant in Drosophila melanogaster.
The biochemical properties of three allozymes coded by the Est-6 locus, two common forms (EST-6S and EST-6F) and one rare form (EST-6VF), were studied. The results show the existence of differences in isoelectric point, activity, activation energy, Km, and temperature coefficient among the three variants, especially between the two common forms and the one rare form. The specific activity of the rare enzymatic variant seems to be less affected by temperature variation. The possible significance of these findings in relation to the mechanism of reproduction is briefly discussed.
D000483:Alleles; D000818:Animals; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000235:genetics*; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics*; D014644:Genetic Variation; D006720:Homozygote; D007527:Isoenzymes / Q000235:genetics* / Q000378:metabolism; D007700:Kinetics; D013816:Thermodynamics
D029721:Drosophila Proteins; D007527:Isoenzymes; D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase; C468266:Est-6 protein, Drosophila