Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta

Dumas, David P.; Durst, H. D.; Landis, Wayne G.; Raushel, Frank M.; Wild, James R.

doi:10.1016/0003-9861(90)90564-f

Cited by 298 publications

(235 citation statements)

References 19 publications

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Section: Introductionmentioning

confidence: 99%

“…The organophosphorus hydrolase has a broad range of substrates and functions at broad pH and temperature (Mulbry et al, 1986), and therefore considered to be useful for the detoxifi cation of the pesticide-polluted environment. Moreover, it has been recently applied to the degradation of nerve agents such as sarin and soman (Dumas et al, 1990) for decontamination in the case of chemical terrorism.In spite of the intensive study of the degrading enzyme, classifi cation of the producer of the enzyme has not attracted attention, and strain ATCC 27551 has been kept as Flavobacterium sp. since the early studies of this bacterium in 1970s (Sethunathan and Yoshida, 1973b).…”

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confidence: 99%

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Reclassification of a parathione-degrading Flavobacterium sp. ATCC 27551 as Sphingobium fuliginis

Kawahara

Tanaka

Yoon

et al. 2010

J. Gen. Appl. Microbiol.

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IntroductionFlavobacterium sp. ATCC 27551 was isolated from paddy fi eld water of the Philippines as a degrader of organophosphorus pesticides such as diazinon and parathion (Sethunathan and Yoshida, 1973a). The pesticides were found to be degraded by organophosphorus hydrolase (Mulbry and Karns, 1989) which was encoded on a 43-kb plasmid (Mulbry et al., 1986). The organophosphorus hydrolase has a broad range of substrates and functions at broad pH and temperature (Mulbry et al., 1986), and therefore considered to be useful for the detoxifi cation of the pesticide-polluted environment. Moreover, it has been recently applied to the degradation of nerve agents such as sarin and soman (Dumas et al., 1990) for decontamination in the case of chemical terrorism.In spite of the intensive study of the degrading enzyme, classifi cation of the producer of the enzyme has not attracted attention, and strain ATCC 27551 has been kept as Flavobacterium sp. since the early studies of this bacterium in 1970s (Sethunathan and Yoshida, 1973b). However, bacterial taxonomy has developed in these several decades and the members of the genus Flavobacterium have been reclassifi ed to other taxa.Sphingomonas was fi rst proposed by Yabuuchi et al. (1990) with fi ve species, but later developed to large group of species, and the new family Sphin- J. Gen. Appl. Microbiol., 56, 249 255 (2010) A parathione-degrading bacterium isolated from rice fi eld in the Philippines, Flavobacterium sp. ATCC 27551 (Sethunathan and Yoshida, 1973, Can. J. Microbiol., 19, 873 875), was re-examined chemotaxonomically and phylogenetically. The strain contained 2-hydroxymyristic acid (2-OH 14 0), cis-vaccenic acid (18 1 ω7c), and palmitic acid (16 0) as major cellular fatty acids, two kinds of glycosphingolipids, and ubiquinone-10 as a sole quinone component. The G+C content of genomic DNA of the strain was 65.9 mol%. The phylogenetic analyses of the 16S rRNA gene indicated that the strain was included in the family Sphingomonadaceae, and most closely related to Sphingobium fuliginis (98.0% similarity) and Sphingobium herbicidovorans (97.3%). The strain showed similar physiological characteristics and a moderate value of DNA DNA relatedness to S. fuliginis. These data suggested it reasonable to conclude that strain ATCC 27551 was identifi ed as S. fuliginis.

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Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

Reclassification of a parathione-degrading Flavobacterium sp. ATCC 27551 as Sphingobium fuliginis

Kawahara

Tanaka

Yoon

et al. 2010

J. Gen. Appl. Microbiol.

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“…strain ATCC 27751 (Mulbry et al 1986;Harper et al 1988;McDaniel et al 1988). Pseudomonas OPH is a dimeric metalloenzyme (35 kDa per monomer) containing 1-2 Zn 2+ or Co 2+ ions per subunit (Dumas et al 1989;Omburo et al 1993). A second enzyme exhibiting high-level DFP-hydrolyzing activity, OPAA-2, was subsequently isolated from the bacterium Alteromonas sp.…”

Section: B Enzymatic Detoxification Of Organophosphorus Compoundsmentioning

confidence: 99%

Structural Analysis and Bioengineering of Thermostable Pyrococcus furiosus Prolidase for the Optimization of Organophosphorus Nerve Agent Detoxification

Du¹,

Grunden²,

Tove³

2012

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Public Reporting Burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing the collection of information. Final Report for "The Structural Analysis and Bioengineering of Thermostable Pyrococcus furiosus Prolidase for Optimization of Organophosphorus Nerve Agent Detoxification"Report Title ABSTRACTThe aims of this project were to structurally study and bioengineer thermostable prolidase from Pyrococcus furiosus to enable its use for oganophosphorus nerve agent detoxification. Prolidase contains one dinuclear Co metal-center/monomer and has optimal activity at 100°C, exhibiting no activity in the absence of Co2+ or at temperatures <50°C. Requirement for metal ions is characteristic of all organophosphorus nerve agent hydrolases and results from these enzymes containing dinuclear metal-centers with one tight-binding metal atom and a second loose-binding metal atom. One primary objective of this study was to determine which of the metal sites is integral and which is labile, information that will be used to bioengineer prolidases. Another objective was to produce P. furiosus prolidase mutants that have increased catalytic activity over a lower range of temperatures using random mutation and a low-temperature selection method. Three mutant prolidases targeting metal-binding amino acids have been successfully produced and biochemical analysis has demonstrated that the Co1 metal-binding site is the high-affinity site and the Co2 site, the low-affinity site. Conditions for selection of mutant prolidases with increased activity at lower temperatures have been determined and mutant prolidases (G39E and E236V) isolated that have higher activity than wild type at 37 °C.

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“…The hydrolysis of coumaphos was determined by wavelength scanning and fluorescence detecting in a 1-cm quartz curette and a 40-well tissue culture plate, respectively, during the incubation of 50 µl protein extract with 1 ml of 0.1 mmol/L coumaphos in 50 mmol/L Tris-HCl (pH 7.0, plus 10% (v/v) methanol) at 37 °C for 30 min. One unit of hydrolysis activity was defined as the production of 1 nmol of chlorferon (3-chloro-4-methyl-7-hydroxycoumarin) per minute under the above conditions based on a calibration curve of chlorferon (98% purity; Sigma-Aldrich, USA) measured at 348 nm (Dumas et al, 1989;Harcourt et al, 2002) by a spectrophotometer (Specord 50; Analytik Jena AG, Germany). The fluorescence was examined and photographed by a gel documentation system (Gel Doc 2000; Bio-Rad, USA) under UV light (ultraviolet rays, approx.…”

Section: Evaluation Of Oph Activitymentioning

confidence: 99%

“…Organophosphorus hydrolase (OPH), encoded by the organophosphorus pesticide degrading (opd) gene, can hydrolyze a wide range of organophosphorus compounds including pesticides, chemical warfare agents, and herbicides (Dumas et al, 1989; Journal of Zhejiang University SCIENCE B ISSN 1673-1581 (Print); ISSN 1862-1783 (Online) www.zju.edu.cn/jzus; www.springerlink.com E-mail: jzus@zju.edu.cn Kolakowski et al, 1997;Di Sioudi et al, 1999). This enzyme has received considerable attention on its use as a bioremediation agent.…”

Section: Introductionmentioning

confidence: 99%

Transient expression of organophosphorus hydrolase to enhance the degrading activity of tomato fruit on coumaphos

Zhao

2009

J. Zhejiang Univ. Sci. B

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Abstract:We constructed an expression cassette of the organophosphorus pesticide degrading (opd) gene under the control of the E8 promoter. Then opd was transformed into tomato fruit using an agroinfiltration transient expression system. β-Glucuronidase (GUS) staining, reverse transcription-polymerase chain reaction (RT-PCR), wavelength scanning, and fluorescent reaction were performed to examine the expression of the opd gene and the hydrolysis activity on coumaphos of organophosphorus hydrolase (OPH) in tomato fruit. The results show that the agroinfiltrated tomato fruit-expressed OPH had the maximum hydrolysis activity of about 11.59 U/mg total soluble protein. These results will allow us to focus on breeding transgenic plants that could not only enhance the degrading capability of fruit and but also hold no negative effects on pest control when spraying organophosphorus pesticides onto the seedlings in fields.

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Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta

Cited by 298 publications

References 19 publications

Reclassification of a parathione-degrading Flavobacterium sp. ATCC 27551 as Sphingobium fuliginis

Reclassification of a parathione-degrading Flavobacterium sp. ATCC 27551 as Sphingobium fuliginis

Structural Analysis and Bioengineering of Thermostable Pyrococcus furiosus Prolidase for the Optimization of Organophosphorus Nerve Agent Detoxification

Transient expression of organophosphorus hydrolase to enhance the degrading activity of tomato fruit on coumaphos

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