Titball R W, Leslie D L, Harvey S, Kelly D
Chemical Defence Establishment, Salisbury, Wiltshire, United Kingdom.
Infect Immun. 1991 May;59(5):1872-4. doi: 10.1128/iai.59.5.1872-1874.1991.
The N-terminal domain of Clostridium perfringens alpha-toxin, homologous with the nontoxic phospholipase C of Bacillus cereus, was expressed in Escherichia coli and shown to retain all of the phosphatidylcholine hydrolyzing activity of the alpha-toxin, but not the sphingomyelinase, hemolytic, or lethal activities. The C-terminal domain of alpha-toxin showed sequence and predicted structural homologies with the N-terminal region of arachidonate 5-lipoxygenase, an enzyme from the human arachidonic acid pathway which plays a role in inflammatory and cardiovascular diseases in humans.
产气荚膜梭菌α毒素的N端结构域与蜡样芽孢杆菌的无毒磷脂酶C同源，在大肠杆菌中表达，结果表明它保留了α毒素的所有磷脂酰胆碱水解活性，但不具有鞘磷脂酶、溶血或致死活性。α毒素的C端结构域与花生四烯酸5-脂氧合酶的N端区域在序列和预测结构上具有同源性，花生四烯酸5-脂氧合酶是一种来自人类花生四烯酸途径的酶，在人类炎症和心血管疾病中起作用。
