IMR Press / FBL / Volume 26 / Issue 4 / DOI: 10.2741/4916

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Hydrolysis of chiral organophosphorus compounds by phosphotriesterases and mammalian paraoxonase-1
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1 Laboratorio de Neuroproteccion, Facultad de Farmacia, Universidad Autonoma del Estado de Morelos, Morelos, Mexico
2 Division de Ciencias Basicas e Ingenierias, Universidad Popular de la Chontalpa, H. Cardenas, Tabasco, Mexico
3 Instituto de Bioingenieria, Universidad Miguel Hernandez, Elche, Alicante, Spain
Send correspondence to: Antonio Monroy-Noyola, Laboratorio de Neuroproteccion, Facultad de Farmacia, Universidad Autonoma del Estado de Morelos, Av. Universidad 1001, Col, Chamilpa C.P. 62209, Cuernavaca, Morelos, Mexico, Tel: 52-777-329-79-89, Fax: 52-777-329-70-89, E-mail:
Front. Biosci. (Landmark Ed) 2021, 26(4), 744–770;
Published: 1 October 2020
(This article belongs to the Special Issue Enviromental medicine and its impact on human health)

Some organophosphorus compounds (OPs), which are used in the manufacturing of insecticides and nerve agents, are racemic mixtures with at least one chiral center with a phosphorus atom. Acute exposure of humans to these mixtures induces the covalent modification of acetylcholinesterase (AChE) and neuropathy target esterase (NTE) and causes a cholinergic syndrome or organophosphate-induced delayed polyneuropathy syndrome (OPIDP). These irreversible neurological effects are due to the stereoselective interaction of the racemic OPs with these B-esterases (AChE and NTE) and such interactions have been studied in vivo, ex vivo and in vitro, using stereoselective hydrolysis by A-esterases or phosphotriesterases (PTEs) and the PTE from Pseudomonas diminuta, and paraoxonase-1 (PON1) from mammalian serum. PON1 has a limited hydrolytic potential of the racemic OPs, while the bacterial PTE exhibits a significant catalytic activity on the less toxic isomers P(+) of the nerve agents. Avian serum albumin also shows a hydrolyzing capacity of chiral OPs with oxo and thio forms. There are ongoing environmental and bioremediation efforts to design and produce recombinants as bio-scavengers of OPs.

Chiral organophosphorus
Calcium. copper
Nervous agent
Figure 1
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