Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Catalytic activities of cocaine hydrolases against the most toxic cocaine metabolite norcocaethylene.

Organic & biomolecular chemistry - 11 Mar 2020

Zheng Xirong, Chen Xiabin, Zhang Ting, Zhan Max, Zhan Chang-Guo, Zheng Fang

Abstract excerpt

A majority of cocaine users also consume alcohol. The concurrent use of cocaine and alcohol produces the pharmacologically active metabolites cocaethylene and norcocaethylene, in addition to norcocaine. Both cocaethylene and norcocaethylene are more toxic than cocaine itself. Hence, a truly valuable cocaine-metabolizing enzyme for cocaine abuse/overdose treatment should be effective for the hydrolysis of not only...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biocatalysis
Share to Butyrylcholinesterase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Carboxylic Ester Hydrolases

Share to Cocaine

Share to Cricetulus

Share to Enzyme Assays

Share to Hydrolysis

Share to Molecular Docking Simulation

Source

Open in PubMed Open full text

Identifiers

PMID: 32101217
DOI: 10.1039/c9ob02762a
PMCID: PMC7362898

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Catalytic activities of cocaine hydrolases against the most toxic cocaine metabolite norcocaethylene.PMID 32101217Read ↗

Amino-acid mutations to extend the biological half-life of a therapeutically valuable mutant of human butyrylcholinesterase.Semantic proximity Read ↗

Substrate selectivity of high-activity mutants of human butyrylcholinesterase.Semantic proximity Read ↗

Characterization of a high-activity mutant of human butyrylcholinesterase against (-)-cocaine.Semantic proximity Read ↗

Rational design of an enzyme mutant for anti-cocaine therapeutics.Semantic proximity Read ↗

Evaluation of the hydrolytic activity of a long-acting mutant bacterial cocaine in the presence of commonly co-administered drugs.Semantic proximity Read ↗

An improved cocaine hydrolase: the A328Y mutant of human butyrylcholinesterase is 4-fold more efficient.Semantic proximity Read ↗

Plant-expressed cocaine hydrolase variants of butyrylcholinesterase exhibit altered allosteric effects of cholinesterase activity and increased inhibitor sensitivity.Semantic proximity Read ↗

Predicted Michaelis-Menten complexes of cocaine-butyrylcholinesterase. Engineering effective butyrylcholinesterase mutants for cocaine detoxication.Semantic proximity Read ↗

Plants as a source of butyrylcholinesterase variants designed for enhanced cocaine hydrolase activity.Semantic proximity Read ↗

Rational design, preparation, and characterization of a therapeutic enzyme mutant with improved stability and function for cocaine detoxification.Semantic proximity Read ↗

Structural analysis of thermostabilizing mutations of cocaine esteraseSemantic proximity Read ↗

Review of human butyrylcholinesterase structure, function, genetic variants, history of use in the clinic, and potential therapeutic uses.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.