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. 1993 Sep;59(9):3138-40.
doi: 10.1128/aem.59.9.3138-3140.1993.

Purification and Properties of a Highly Active Organophosphorus Acid Anhydrolase from Alteromonas undina

T C Cheng  1 , S P Harvey, A N Stroup
Affiliations

Purification and Properties of a Highly Active Organophosphorus Acid Anhydrolase from Alteromonas undina

T C Cheng et al. 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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