enzyme reactivation
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Biomolecules ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 583 ◽  
Author(s):  
Daniel Kitagawa ◽  
Samir Cavalcante ◽  
Reuel de Paula ◽  
Rafael Rodrigues ◽  
Leandro Bernardo ◽  
...  

Casualties caused by organophosphorus pesticides are a burden for health systems in developing and poor countries. Such compounds are potent acetylcholinesterase irreversible inhibitors, and share the toxic profile with nerve agents. Pyridinium oximes are the only clinically available antidotes against poisoning by these substances, but their poor penetration into the blood-brain barrier hampers the efficient enzyme reactivation at the central nervous system. In searching for structural factors that may be explored in future SAR studies, we evaluated neutral aryloximes as reactivators for paraoxon-inhibited Electrophorus eel acetylcholinesterase. Our findings may result into lead compounds, useful for development of more active compounds for emergencies and supportive care.


Author(s):  
Elspeth J. Hulse ◽  
Michael Eddleston

Poisoning with agricultural chemicals is common in rural Asia-Pacific with up to 300,000 annual deaths from pesticide self-poisoning. The pharmacokinetics and pharmacodynamics of pesticides can vary markedly depending on the chemicals ingested, the pesticide’s lipid solubility, enzyme reactivation, co-ingested toxicants, and extent of decontamination and organ dysfunction. Diagnosis and management is based on clinical signs and standard investigations. Staff should wear standard universal precaution attire for examining and treating patients; nosocomial poisoning is rare. Management of poisonings should include careful airway intervention and administration of oxygen, except in suspected paraquat poisoning. Organophosphorus insecticide poisoning causes a cholinergic crisis with excess airway secretions and acute respiratory failure. Patients should be treated with intravenous atropine and observed for the neuromuscular disorder ‘intermediate syndrome’, which can cause further paralysis and respiratory failure after 24 hours. Few antidotes exist for other agricultural chemical poisonings with the mainstay of treatment being supportive standard ICU care.


2015 ◽  
Vol 32 (1) ◽  
pp. 54-59 ◽  
Author(s):  
Carola Bahamondes ◽  
Lorena Wilson ◽  
Claudia Bernal ◽  
Andrés Illanes ◽  
Gregorio Álvaro ◽  
...  
Keyword(s):  

2012 ◽  
Vol 59 (2) ◽  
Author(s):  
Dimo Dimov ◽  
Kamen Kanev ◽  
Ivanka Dimova

Butyrylcholinesterase (BChE) is synthesized in the liver and found in high concentrations in blood plasma, liver, heart, pancreas, vascular endothelium, skin, brain white matter, smooth muscle cells and adipocytes. BChE is a non specific enzyme that hydrolyzes different choline esters (succinylcholine, mivacurium) and many other drugs such as aspirin, cocaine and procaine. The enzyme is also considered as a bioscavenger due to its ability to neutralize the toxic effects of organophosphorus compounds (nervous system fs agents) such as soman. BChE displays several polymorphisms that influence its serum activity; therefore they could determine the individual sensitivity to chemical nerve agents. In this study, we investigated the correlation between BChE variants and the degree of enzyme inhibition and reactivation after soman application on blood samples of 726 individuals. The blood samples of individuals expressing abnormal variants, were more sensitive to soman compared to variants of homozygotes and heterozygotes for U-allele. We found significant differences in the degree of enzyme reactivation between different variants (with and without U-presence).


2011 ◽  
Vol 286 (30) ◽  
pp. 26541-26554 ◽  
Author(s):  
Rong Fu ◽  
Rupal Gupta ◽  
Jiafeng Geng ◽  
Kednerlin Dornevil ◽  
Siming Wang ◽  
...  

2007 ◽  
Vol 27 (13) ◽  
pp. 4774-4783 ◽  
Author(s):  
G. D. Vivek Sagar ◽  
Balázs Gereben ◽  
Isabelle Callebaut ◽  
Jean-Paul Mornon ◽  
Anikó Zeöld ◽  
...  

ABSTRACT Ubiquitination is a critical posttranslational regulator of protein stability and/or subcellular localization. Here we show that ubiquitination can also regulate proteins by transiently inactivating enzymatic function through conformational change in a dimeric enzyme, which can be reversed upon deubiquitination. Our model system is the thyroid hormone-activating type 2 deiodinase (D2), an endoplasmic reticulum-resident type 1 integral membrane enzyme. D2 exists as a homodimer maintained by interacting surfaces at its transmembrane and globular cytosolic domains. The D2 dimer associates with the Hedgehog-inducible ubiquitin ligase WSB-1, the ubiquitin conjugase UBC-7, and VDU-1, a D2-specific deubiquitinase. Upon binding of T4, its natural substrate, D2 is ubiquitinated, which inactivates the enzyme by interfering with D2's globular interacting surfaces that are critical for dimerization and catalytic activity. This state of transient inactivity and change in dimer conformation persists until deubiquitination. The continuous association of D2 with this regulatory protein complex supports rapid cycles of deiodination, conjugation to ubiquitin, and enzyme reactivation by deubiquitination, allowing tight control of thyroid hormone action.


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