Abstract
PhospholipaseA2 is the first enzyme in the eicosanoids pathway. PLA2 from various species have been characterized and classified into several groups. Differential expression and functions of these different groups are yet to be established. Among these, the group I and II PLA2s have been studied most. We report here our results on the cloning and sequencing of PLA2s from Indian red and black scorpions and the expression of red scorpion PLA2 in bacterial system. The expressed protein was purified from the inclusion bodies in its active form. Amino acid comparisons establish that scorpion PLA2 belongs to group III and does not have sequence homology with other PLA2 groups. The nucleotide homology with other group III PLA2 also is not significant. However the sequence motifs for the catalysis, for Ca++ binding as well as for the secondary structures are well conserved. It has a truncated N-terminus and an extended C-terminal sequence. The extended C-terminal segment does not display any sequence homology to ...
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