Purification and Properties of a Highly Active Organophosphorus Acid Anhydrolase from Alteromonas undina
- 1 September 1993
- journal article
- research article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 59 (9) , 3138-3140
- https://doi.org/10.1128/aem.59.9.3138-3140.1993
Abstract
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. ImagesKeywords
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