Gas-phase stability and thermodynamics of ligand-bound, binary complexes of chloramphenicol acetyltransferase reveal negative cooperativity.
Chloramphenicol acetyltransferase (CAT)
Collision-induced dissociation (CID)
Collision-induced unfolding (CIU)
Ligand binding
Mass spectrometry (MS)
Protein stability
Journal
Analytical and bioanalytical chemistry
ISSN: 1618-2650
Titre abrégé: Anal Bioanal Chem
Pays: Germany
ID NLM: 101134327
Informations de publication
Date de publication:
Oct 2023
Oct 2023
Historique:
received:
12
05
2023
accepted:
24
07
2023
revised:
17
07
2023
medline:
9
10
2023
pubmed:
6
8
2023
entrez:
5
8
2023
Statut:
ppublish
Résumé
The biological role of the bacterial chloramphenicol (Chl)-resistance enzyme, chloramphenicol acetyltransferase (CAT), has seen renewed interest due to the resurgent use of Chl against multi-drug-resistant microbes. This looming threat calls for more rationally designed antibiotic derivatives that have improved antimicrobial properties and reduced toxicity in humans. Herein, we utilize native ion mobility spectrometry-mass spectrometry (IMS-MS) to investigate the gas-phase structure and thermodynamic stability of the type I variant of CAT from Escherichia coli (EcCAT
Identifiants
pubmed: 37542535
doi: 10.1007/s00216-023-04891-5
pii: 10.1007/s00216-023-04891-5
doi:
Substances chimiques
Chloramphenicol O-Acetyltransferase
EC 2.3.1.28
Ligands
0
Acetyl Coenzyme A
72-89-9
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
6201-6212Subventions
Organisme : NIGMS NIH HHS
ID : 1R15GM146188-01
Pays : United States
Organisme : NIGMS NIH HHS
ID : 1R15GM146188-01
Pays : United States
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH, DE part of Springer Nature.
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