Abstract
Organophosphorus compounds (OPCs) are able to interact with various biological targets in living organisms, including enzymes. The binding of OPCs to enzymes does not always lead to negative consequences for the body itself, since there are a lot of natural biocatalysts that can catalyze the chemical transformations of the OPCs via hydrolysis or oxidation/reduction and thereby provide their detoxification. Some of these enzymes, their structural differences and identity, mechanisms, and specificity of catalytic action are discussed in this work, including results of computational modeling. Phylogenetic analysis of these diverse enzymes was specially realized for this review to emphasize a great area for future development(s) and applications.
Highlights
Organophosphorus compounds (OPCs) are extremely dangerous and have a wide variety of chemical structures mainly presented by phosphotriester, thiophosphotriester, and phosphorothioester moieties [1]
From soil bacteria Agrobacterium radiobacter (OpdA), which has more than 90% amino acid sequence identity and completely identical structure of the active center (Figure 1b), using magnetic circular dichroism has showed [20] that the water molecule bound to the α-metal in the Co2+ -containing enzyme can serve as an attacking nucleophile instead of a hydroxyl group at elevated pH values
A great number of enzymes studied to date and capable of detoxifying OPCs have diverse structures and mechanisms of catalytic action
Summary
Organophosphorus compounds (OPCs) are extremely dangerous and have a wide variety of chemical structures mainly presented by phosphotriester, thiophosphotriester, and phosphorothioester moieties [1]. That totally leads to multiple dysfunctions of cellular regulation [6], oxidative stress, and apoptosis [7] To avoid these negative outcomes, biocatalytic detoxification of OPCs seems to be the most reliable. Despite the structural diversity of OPCs, a large number of enzymes have been discovered to be catalytically active with these compounds. Most of these enzymes (organophosphorus hydrolase, OPH; methyl parathion hydrolase, MPH; organophosphorus acid anhydrolase, OPAA; etc.) belong to hydrolases (Figure 1), but there are oxidoreductases and lyases and some representative examples of these enzyme classes will be discussed later. The purpose of this work was to review and consolidate current literature data about enzymes being catalytically active with OPCs, to emphasize modern approaches to OPCs’. Though there are a lot of other recent reviews on the topic [8,9,10], additional efforts were applied in this work to see the problem wider and possibly generate novel knowledge
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