Pre-Steady-State and Steady-State Kinetic Analysis of Butyrylcholinesterase-Catalyzed Hydrolysis of Mirabegron, an Arylacylamide Drug.
arylacylamide
burst
butyrylcholinesterase
drug metabolism
hysteretic enzyme
mirabegron
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
16 May 2024
16 May 2024
Historique:
received:
20
04
2024
revised:
13
05
2024
accepted:
14
05
2024
medline:
25
5
2024
pubmed:
25
5
2024
entrez:
25
5
2024
Statut:
epublish
Résumé
The β-adrenergic drug Mirabegron, a drug initially used for the treatment of an overactive bladder, has new potential indications and is hydrolyzed by butyrylcholinesterase (BChE). This compound is one of the only arylacylamide substrates to be catabolized by BChE. A steady-state kinetic analysis at 25 °C and pH 7.0 showed that the enzyme behavior is Michaelian with this substrate and displays a long pre-steady-state phase characterized by a burst. The induction time,
Identifiants
pubmed: 38792217
pii: molecules29102356
doi: 10.3390/molecules29102356
pii:
doi:
Substances chimiques
mirabegron
MVR3JL3B2V
Butyrylcholinesterase
EC 3.1.1.8
Acetanilides
0
Thiazoles
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Kazan Federal University
ID : Priority 2030