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Literature DB >> 2001997

Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate.

Abstract

A moderately halophilic bacterial isolate has been found to possess high levels of enzymatic activity against several highly toxic organophosphorus compounds. The predominant enzyme, designated organophosphorus acid anhydrase 2, has been purified 1,000-fold to homogeneity and characterized. The enzyme is a single polypeptide with a molecular weight of 60,000. With diisopropylfluorophosphate as a substrate, the enzyme has optimum activity at pH 8.5 and 50 degrees C, and it is stimulated by manganese and cobalt.

Entities: Chemical

Mesh：

Substances：

Year: 1991 PMID： 2001997 PMCID： PMC207724 DOI： 10.1128/jb.173.6.1938-1943.1991

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

4 in total

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22 in total

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Authors: Ilona Petrikovics; Melinda Wales; Marianna Budai; Jorn C C Yu; Mária Szilasi
Journal: AAPS PharmSciTech Date: 2011-12-09 Impact factor: 3.246

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Authors: Karla Alejo-González; Erik Hanson-Viana; Rafael Vazquez-Duhalt
Journal: J Pestic Sci Date: 2018-02-28 Impact factor: 1.519

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Authors: Andrea Štěpánková; Jarmila Dušková; Tereza Skálová; Jindřich Hašek; Tomáš Koval'; Lars H Østergaard; Jan Dohnálek
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Date: 2013-03-28

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Journal: Protein J Date: 2016-12 Impact factor: 2.371

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