doi: 10.1128/aem.59.9.3138-3140.1993.
Purification and Properties of a Highly Active Organophosphorus Acid Anhydrolase from Alteromonas undina
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- PMID: 16349054
- PMCID: PMC182420
- DOI: 10.1128/aem.59.9.3138-3140.1993
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Purification and Properties of a Highly Active Organophosphorus Acid Anhydrolase from Alteromonas undina
Appl Environ Microbiol.
1993 Sep.
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 approximately 575 mumol/min/mg of protein. The enzyme has optimum activity at pH 8.0 and 55 degrees 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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