Purification and Properties of a Highly Active Organophosphorus Acid Anhydrolase from Alteromonas undina-Reference-Cited by-同舟云学术

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

Published:1993-09 Issue:9 Volume:59 Page:3138-3140
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Cheng Tu-Chen¹,Harvey Steven P.¹,Stroup Adam N.¹

Affiliation:

1. U.S. Army Chemical and Biological Defense Agency, Edgewood Research, Development and Engineering Center, Research and Technology Directorate, Aberdeen Proving Ground, Maryland 21010-5423

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.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/aem.59.9.3138-3140.1993

Reference10 articles.

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