Some biochemical properties of δ-aminolevulinic acid dehydratase in Gammarus pulex

The determination of δ-aminolevulinic acid dehydratase (ALAD; porphobilinogen synthetase, EC 4.2.1.24) activity in aquatic organisms might be a useful marker for the identification of lead exposure. ALADs from the variety of different sources have been grouped into two classes based on some biochemical properties such as molecular weight, pH optimum, metal requirement and susceptibility to EDTA. The first group includes the enzymes from mammals and birds, while the second group ALADs are derived primarily from bacteria and yeasts. In this study, we have characterized Gammarus ALAD in some biochemical aspects. Gammarus pulex were collected from the Porsuk River at Eskişehir (Turkey). The effect of pH, incubation temperature of reaction mixture, incubation period, metal ions and EDTA on enzyme activity were investigated. Comparisons between groups were performed by analysis of a paired t-test. Gammarus ALAD was found biochemically distinct from the mammalian enzyme. It seems to be considered in Class II rather than Class I.