Title : Resolving pathways of interaction of mipafox and a sarin analog with human acetylcholinesterase by kinetics, mass spectrometry and molecular modeling approaches.

Pub. Date : 2016 Mar

PMID : 25743373






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The hydroxyl oxygen of the catalytic triad serine in the active center of serine hydrolase acetylcholinesterase (AChE) attacks organophosphorus compounds (OPs) at the phosphorus atom to displace the primary leaving group and to form a covalent bond. Serine acetylcholinesterase (Cartwright blood group) Homo sapiens
2 The hydroxyl oxygen of the catalytic triad serine in the active center of serine hydrolase acetylcholinesterase (AChE) attacks organophosphorus compounds (OPs) at the phosphorus atom to displace the primary leaving group and to form a covalent bond. Serine acetylcholinesterase (Cartwright blood group) Homo sapiens
3 Inhibited AChE can be reactivated by cleavage of the Ser-phosphorus bond either spontaneously or through a reaction with nucleophilic agents, such as oximes. Serine acetylcholinesterase (Cartwright blood group) Homo sapiens
4 A peptide fingerprinted mass spectrometry (MS) method, which clearly distinguished the peptide with the active serine (active center peptide, ACP) of the human AChE adducted with OPs, was developed by MALDI-TOF and MALDI-TOF/TOF. Serine acetylcholinesterase (Cartwright blood group) Homo sapiens