A highly active organophosphorus acid anhydrolase from Alteromonas undina was purified to homogeneity and found to be composed of a single polypeptide chain with a molecular weight of 53,000. With diisopropylfluorophosphate as a substrate, the purified enzyme has a specific activity of ∼575 μmol/min/mg of protein. The enzyme has optimum activity at pH 8.0 and 55°C and is stimulated by sulfhydryl reducing agents and manganese. It is capable of rapidly hydrolyzing a wide range of nerve agents and several chromogenic phosphinates.
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机译：将来自云纹墨单胞菌（Alteromonas undina）的高活性有机磷酸脱水酶纯化至均质，发现其由分子量为53,000的单条多肽链组成。以二异丙基氟磷酸盐为底物，纯化的酶具有约575μmol/ min / mg蛋白质的比活。该酶在pH 8.0和55°C下具有最佳活性，并被巯基还原剂和锰刺激。它能够迅速水解多种神经毒剂和几种生色次膦酸酯。
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