Organophosphorus Cholinesterase Inhibitors: Detoxification by Microbial Enzymes

DeFrank, Joseph

doi:10.1007/978-1-4757-9235-5_13

Cited by 19 publications

(19 citation statements)

References 71 publications

(34 reference statements)

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“…A number of enzymes exist that are capable of degrading a wide range of OP compounds (69,70). The first OP-degrading enzyme was observed by Mazur, who reported the hydrolysis of DFP to hydrofluoric acid and diisopropylphosphoric acid by enzymes found in the tissues of humans and rabbits (69,71). Since this report, a wide number of bacteria and eukaryotic organisms have been shown to possess the ability to degrade OP compounds (69,71).…”

Section: Biological Meansmentioning

confidence: 99%

“…Furthermore, methods such as incineration and the toxic, corrosive, and flammable nature of many decontamination solutions are not amenable for use over large areas or on sensitive equipment or personnel. For these reasons, there has been vast interest in using biological means of bioremediation for the detoxification of OP compounds (68)(69)(70). A number of enzymes exist that are capable of degrading a wide range of OP compounds (69,70).…”

Section: Biological Meansmentioning

confidence: 99%

“…For these reasons, there has been vast interest in using biological means of bioremediation for the detoxification of OP compounds (68)(69)(70). A number of enzymes exist that are capable of degrading a wide range of OP compounds (69,70). The first OP-degrading enzyme was observed by Mazur, who reported the hydrolysis of DFP to hydrofluoric acid and diisopropylphosphoric acid by enzymes found in the tissues of humans and rabbits (69,71).…”

Section: Biological Meansmentioning

confidence: 99%

See 2 more Smart Citations

Biomaterials for Mediation of Chemical and Biological Warfare Agents

Russell

Berberich²,

Drevon³

et al. 2003

Annu. Rev. Biomed. Eng.

187

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Recent events have emphasized the threat from chemical and biological warfare agents. Within the efforts to counter this threat, the biocatalytic destruction and sensing of chemical and biological weapons has become an important area of focus. The specificity and high catalytic rates of biological catalysts make them appropriate for decommissioning nerve agent stockpiles, counteracting nerve agent attacks, and remediation of organophosphate spills. A number of materials have been prepared containing enzymes for the destruction of and protection against organophosphate nerve agents and biological warfare agents. This review discusses the major chemical and biological warfare agents, decontamination methods, and biomaterials that have potential for the preparation of decontamination wipes, gas filters, column packings, protective wear, and self-decontaminating paints and coatings.

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Section: Biological Meansmentioning

confidence: 99%

Section: Biological Meansmentioning

confidence: 99%

Section: Biological Meansmentioning

confidence: 99%

See 1 more Smart Citation

Biomaterials for Mediation of Chemical and Biological Warfare Agents

Russell

Berberich²,

Drevon³

et al. 2003

Annu. Rev. Biomed. Eng.

187

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“…are hydrophobic phosphorus (V) esters or phosphylating agents. They can irreversibly react with the enzyme acetylcholinesterase (AChE), inhibiting its control over the central nervous system [1][2][3]. AChE catalyzes the ester hydrolysis process of the neurotransmitter acetylcholine (ACh) to terminate synaptic transmission [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Probing the reactivation process of sarin-inhibited acetylcholinesterase with α-nucleophiles: Hydroxylamine anion is predicted to be a better antidote with DFT calculations

Khan

Bandyopadhyay

et al. 2011

Journal of Molecular Graphics and Modelling

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“…The most studied organophosphate esterase is the monoesterase alkaline phosphatase (16). Recently, there has been significant interest in phophotriesterases because of their ability to detoxify the organophosphate triester nerve agents and pesticides (6,18). The phosphodiesterases remain the least studied of the phosphoesterases.…”

mentioning

confidence: 99%

Gene Cloning, Purification, and Characterization of a Phosphodiesterase from Delftia acidovorans

Tehara

Keasling

2003

Appl Environ Microbiol

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A novel phosphodiesterase (PdeA) was purified from Delftia acidovorans, the gene encoding the enzyme was cloned and expressed in Escherichia coli, and the recombinant enzyme was purified to apparent homogeneity and characterized. PdeA is an 85-kDa trimer that exhibits maximal activity at 65°C and pH 10 even though it was isolated from a mesophilic bacterium. Although PdeA exhibited both mono-and diesterase activity, it was most active on the phosphodiester bis(p-nitrophenyl)phosphate with a K m of 2.9 ؎ 0.1 mM and a k cat of 879 ؎ 73 min ؊1 . The enzyme showed sequence similarity to cyclic AMP (cAMP) phosphodiesterase and cyclic nucleotide phosphodiesterases and exhibited activity on cAMP in vivo when the gene was expressed in E. coli. The IS1071 transposon insertion sequence was found downstream of pdeA.Biological systems use organophosphates as energy carriers, signaling molecules, and major components of the cell (DNA, RNA, and phospholipids). As such, organisms contain a number of organophosphate esterases to regulate the levels of these compounds. Due to the low solubility of inorganic phosphate in the environment, organisms also produce organophosphate esterases to liberate inorganic phosphate for use in growth. The most studied organophosphate esterase is the monoesterase alkaline phosphatase (16). Recently, there has been significant interest in phophotriesterases because of their ability to detoxify the organophosphate triester nerve agents and pesticides (6, 18). The phosphodiesterases remain the least studied of the phosphoesterases.Phosphodiesterases from mammalian sources have attracted some attention due to their importance in regulation (19). These phosphodiesterases are high-affinity enzymes, whereas phosphodiesterases from bacterial sources show much lower affinities (12). Bacterial phosphodiesterases have been purified from a variety of sources including Escherichia coli (10), Haemophilus influenzae (14), and Burkholderia caryophylli PG2982 (7). The phosphodiesterases from E. coli and H. influenzae are similar in sequence, and both moderate intracellular cyclic AMP (cAMP) levels. A phosphodiesterase with no sequence similarity to the enzymes of E. coli and H. influenzae that was isolated from B. caryophylli PG2982 initially for its monoesterase activity was later found to have diesterase activity (7). This enzyme could not be clearly ascribed a function but was thought to play a role in a xenobiotic degradation pathway because it degraded glycerol glyphosate.Delftia acidovorans (formerly Comamonas acidovorans), originally isolated from a waste treatment facility, can utilize diethylphosphate (DEP) and diethylthiophosphate as sole sources of phosphorus (5). To date, the phosphodiesterase responsible for this activity has not been isolated or cloned.Since many organophosphate xenobiotics such as pesticides and chemical warfare agents contain ester bonds, this phosphodiesterase could be applied to biodegradation of this class of pollutants. Other enzymes isolated from D. acidovorans have been impl...

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Organophosphorus Cholinesterase Inhibitors: Detoxification by Microbial Enzymes

Cited by 19 publications

References 71 publications

Biomaterials for Mediation of Chemical and Biological Warfare Agents

Biomaterials for Mediation of Chemical and Biological Warfare Agents

Probing the reactivation process of sarin-inhibited acetylcholinesterase with α-nucleophiles: Hydroxylamine anion is predicted to be a better antidote with DFT calculations

Gene Cloning, Purification, and Characterization of a Phosphodiesterase from Delftia acidovorans

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