DeFrank_1991_J.Bacteriol_173_1938

Reference

Title : Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate - DeFrank_1991_J.Bacteriol_173_1938
Author(s) : DeFrank JJ , Cheng TC
Ref : Journal of Bacteriology , 173 :1938 , 1991
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.

PubMedSearch : DeFrank_1991_J.Bacteriol_173_1938
PubMedID: 2001997

Related information

Citations formats

DeFrank JJ, Cheng TC (1991)
Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate
Journal of Bacteriology 173 :1938

DeFrank JJ, Cheng TC (1991)
Journal of Bacteriology 173 :1938