Human Plasma Butyrylcholinesterase Hydrolyzes Atropine: Kinetic and Molecular Modeling Studies.


Journal

Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009

Informations de publication

Date de publication:
04 May 2024
Historique:
received: 05 04 2024
revised: 29 04 2024
accepted: 02 05 2024
medline: 11 5 2024
pubmed: 11 5 2024
entrez: 11 5 2024
Statut: epublish

Résumé

The participation of butyrylcholinesterase (BChE) in the degradation of atropine has been recurrently addressed for more than 70 years. However, no conclusive answer has been provided for the human enzyme so far. In the present work, a steady-state kinetic analysis performed by spectrophotometry showed that highly purified human plasma BChE tetramer slowly hydrolyzes atropine at pH 7.0 and 25 °C. The affinity of atropine for the enzyme is weak, and the observed kinetic rates versus the atropine concentration was of the first order: the maximum atropine concentration in essays was much less than

Identifiants

pubmed: 38731631
pii: molecules29092140
doi: 10.3390/molecules29092140
pii:
doi:

Substances chimiques

Butyrylcholinesterase EC 3.1.1.8
Atropine 7C0697DR9I

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Kazan Federal University
ID : Priority 2030
Organisme : Government of India
ID : BT/INF/22/SP45375/2022

Auteurs

Aliya Mukhametgalieva (A)

Laboratory of Biochemical Neuropharmacology, Kazan Federal University, Kremlevskaya Str. 18, 420008 Kazan, Russia.

Showkat Ahmad Mir (SA)

School of Life Sciences, Sambalpur University, Jyotivihar, Burla 768019, India.

Zukhra Shaihutdinova (Z)

Laboratory of Biochemical Neuropharmacology, Kazan Federal University, Kremlevskaya Str. 18, 420008 Kazan, Russia.

Patrick Masson (P)

Laboratory of Biochemical Neuropharmacology, Kazan Federal University, Kremlevskaya Str. 18, 420008 Kazan, Russia.

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Classifications MeSH