Alteromonas prolidase for organophosphorus G-agent decontamination

Cheng, Tu-Chen; DeFrank, Joseph; Rastogi, Vipin K.

doi:10.1016/s0009-2797(99)00058-7

Cited by 95 publications

(52 citation statements)

References 8 publications

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“…Currently there are many studies ongoing to design effective methods to remove pesticides from the environment, in particular a rapid increase in the field of bioremediation has been observed, principally based on the use of free enzymes [33][34][35] and microorganisms [36]. Encouraging results has been obtained but they are not applicable on a large scale, therefore the development of these new technologies is important but the rational use of pesticides and the control of industrial and urban waste is essential to preserve wildlife and human health.…”

Section: From Researchmentioning

confidence: 99%

Endocrine Disrupters: The Hazards for Human Health

2013

Clon Transgen

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In last decades an increasing number of cases have been described in humans and wildlife ascribed to the effects of xenobiotics compounds which interfere with hormonal system. Generically, these compounds are described as endocrine disrupters; due to their potential hazard they have received great attention by the scientific community and the media. In this brief editorial will be considered some general aspect, and in particular related to a class of endocrine disrupters: the organophosphate pesticides.

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Section: From Researchmentioning

confidence: 99%

Endocrine Disrupters: The Hazards for Human Health

2013

Clon Transgen

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“…However, only OPAA-2 can degrade the nerve agent soman (Cheng, Harvey et al 1996). Like OPH, OPAA-2 has been cloned and overexpressed and additionally has been successfully incorporated into foams used for the decontamination of OP-contaminated surfaces (Cheng et al 1999).…”

Section: B Enzymatic Detoxification Of Organophosphorus Compoundsmentioning

confidence: 99%

“…3.4.13.9), dipeptidases specific for hydrolyzing a dipeptide bond with a prolyl residue at the C-terminus [X-Pro] (Cheng, Harvey et al 1996;Cheng, Liu et al 1997). It is thought that the ability of the OPAA enzymes to hydrolyze P-F, P-O, P-CN, and P-S bonds in toxic OP compounds may arise from the fortuitous similarity of these compounds in shape, size and surface charges to the true prolidase X-Pro dipeptide substrates (Cheng, Harvey et al 1996;Cheng, DeFrank et al 1999) …”

Section: Prolidases Can Hydrolyze Toxic Organophosphorus Compoundsmentioning

confidence: 99%

“…Based on work by Cheng and Defrank, the use of prolidases to detoxify OP nerve agent contamination has become feasible (Cheng et al 1999). However, there remain questions in regards to the exact nature of the metal centers in prolidases, the identity of the amino acid residues that participate in substrate binding to these enzymes, as well as confirmation of the predicted reaction mechanism used by the enzyme.…”

Section: Statement Of the Problem Studiedmentioning

confidence: 99%

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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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“…Enzymatic degradation of OPs was considered as a desirable decontamination method with many advantages, such as being economic, efficient and environmentally friendly (Singh and Walker 2006). A number of enzymes capable of degrading OPs have been discovered during the past years, including organophosphorus acid anhydrolases (OPAAs; EC 3.4.13.9) (Cheng et al 1999;Vyas et al 2010), phosphotriesterases (PTEs; EC 3.1.8.1) (Omburo et al 1992), paraoxonases (PONs; EC 3.1.8.1) (Ben-David et al 2012), phosphotriesterase-like lactonases (PLLs; EC 3.1.1.81) (Afriat et al 2006), and methyl-parathion hydrolases (MPHs; EC 3.1.8.1) (Hong et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Marked enhancement of Acinetobacter sp. organophosphorus hydrolase activity by a single residue substitution Ile211Ala

Chen

Luo

Chen

et al. 2015

Bioresour. Bioprocess.

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Background:The activity of organophosphorus hydrolase (OPH) that catalyzes the hydrolysis of neurotoxic organophosphates (OPs) was reported to evolve from lactonase. Results:In this study, a putative OPH from Acinetobacter sp. (AbOPH) exhibited high lactonase activity with latent OPH activity. Sequence alignment and phylogenetic tree analysis revealed the unique status of AbOPH in evolution. The crystal structure of AbOPH was determined at 2.0 Å resolution and a semi-rational design was performed to enhance the OPH activity of AbOPH through a consensus sequence approach. Compared with wild-type AbOPH, which exhibited undetectable activity toward methyl-parathion (MP), the best variant AbOPH I211A showed markedly improved catalytic efficiency (1.1 μmol min −1 mg −1 protein ) toward MP. Docking studies suggested that the mutation Ile211Ala affects substrate recognition and stabilizes substrate conformation. Conclusions:This result presents the emergence of new enzyme function by a simple mutation strategy and confirms the high possibility that OPH was evolved from its lactonase ancestor.

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Alteromonas prolidase for organophosphorus G-agent decontamination

Cited by 95 publications

References 8 publications

Endocrine Disrupters: The Hazards for Human Health

Endocrine Disrupters: The Hazards for Human Health

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

Marked enhancement of Acinetobacter sp. organophosphorus hydrolase activity by a single residue substitution Ile211Ala

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