Abstract
AbstractThe enzyme phospholipase A2 (EC 3.1.1.4; PLA2) is widely distributed among various species in the animal kingdom, notably in the pancreatic tissues of mammals and animal venoms of reptiles and insects. It catalyzes efficiently and specifically the hydrolysis of the 2-acyl ester bond in 3-sn-phosphoglycerides. The primary sequences of more than 100 PLA2 from various tissues of different animal families have been solved. Based on their primary structure, PLA2s are classified into two groups. Group I comprises those from mammalian pancreas and the venoms of snake families Elapidae and Hydrophidae. The Group II PLA2s those from the venoms of Crotalidae and Viperidae, have a short extension at the carboxyl terminus that terminates in a half-cystine linked to a half-cystine near the active site at position 50. Despite these structural differences, the PLA2S are homologous proteins which show considerable sequence similarity, particularly in the Ca2+-binding and active site regions.Besides a catalyst for...
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