Abstract
The organophosphorus substances, including pesticides and nerve agents (NAs), represent highly toxic compounds. Standard decontamination procedures place a heavy burden on the environment. Given their continued utilization or existence, considerable efforts are being made to develop environmentally friendly methods of decontamination and medical countermeasures against their intoxication. Enzymes can offer both environmental and medical applications. One of the most promising enzymes cleaving organophosphorus compounds is the enzyme with enzyme commission number (EC): 3.1.8.2, called diisopropyl fluorophosphatase (DFPase) or organophosphorus acid anhydrolase from Loligo Vulgaris or Alteromonas sp. JD6.5, respectively. Structure, mechanisms of action and substrate profiles are described for both enzymes. Wild-type (WT) enzymes have a catalytic activity against organophosphorus compounds, including G-type nerve agents. Their stereochemical preference aims their activity towards less toxic enantiomers of the chiral phosphorus center found in most chemical warfare agents. Site-direct mutagenesis has systematically improved the active site of the enzyme. These efforts have resulted in the improvement of catalytic activity and have led to the identification of variants that are more effective at detoxifying both G-type and V-type nerve agents. Some of these variants have become part of commercially available decontamination mixtures.
Highlights
Biological decomposition of toxic substances has become a very attractive topic
As the nomenclature of these enzymes was unsystematic and confusing, the literature soon became became filled with references to phosphorylphosphatase, fluorophosphatase, diisopropyl fluorophosphatase (DFPase), paraoxon, filled with references to phosphorylphosphatase, fluorophosphatase, DFPase, paraoxon, parathion parathion hydrolase, phosphotriesterase, phosphofluorase, somanase, sarinase, and tabunase
It increases the partial to this mechanism, thephosphorus incoming substrate is replaced by athe calcium coordinating in positive charge of the atom, which facilitates nucleophilic attackwater of themolecule hydrolytic the active site
Summary
Biological decomposition of toxic substances has become a very attractive topic. At present, particular emphasis is placed on industrial processes and technologies that do not burden the environment but help to clean or protect it. Biodegradation is defined as a process of decomposing toxic compounds by living organisms without producing other hardly degradable substances. According to the World Health Organization, there are three million pesticide poisonings every year [6]. Another part of this issue is the possibility that these substances leak into the ground and enter municipal water supplies and pollute the surrounding environment. Several enzymes from different kinds of organisms (bacteria, protozoa, squid, clams, and mammals) have been reported to cleave and detoxify specific groups of pesticides and NA These enzymes, with varying esterase specificities, have been designated as phosphoric triester hydrolases (EC: 3.1.8) with two subgroups, including aryldialkylphosphatase (EC: 3.1.8.1), called phosphotriesterase (PTE). DFPase and OPAA will be a subject of this article
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
