Human Plasma Butyrylcholinesterase Hydrolyzes Atropine: Kinetic and Molecular Modeling Studies.
atropine
atropinesterase
butyrylcholinesterase
molecular dynamics
steady-state hydrolysis
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
04 May 2024
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