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.
MeSH Terms
Antibodies, Monoclonal/immunology
Bacterial Proteins/immunology,isolation & purification
Blotting, Western
Chromatography
Esterases
Gram-Negative Bacteria/enzymology,immunology
Hydrogen-Ion Concentration
Hydrolases/antagonists & inhibitors,isolation & purification,metabolism
Kinetics
Metals/pharmacology
Molecular Weight
Organophosphorus Compounds/metabolism
Phosphoric Triester Hydrolases
Substrate Specificity
Sulfhydryl Reagents/pharmacology
Temperature
Chemicals
Antibodies, Monoclonal
Bacterial Proteins
Metals
Organophosphorus Compounds
Sulfhydryl Reagents
diisopropylphosphate
Hydrolases
Esterases
Phosphoric Triester Hydrolases
diisopropyl-fluorophosphatase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
DeFrank J J
U.S. Army Chemical Research, Development & Engineering Center, Aberdeen Proving Ground, Maryland 21010-5423.
Cheng T C
References (4)
4 references, click to expand
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PMID: 4004925
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