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Gas-phase stability and thermodynamics of ligand-bound, binary complexes of chloramphenicol acetyltransferase reveal negative cooperativity

ABSTRACT: Bottom-up proteomics confirms the identity of protein at EcCATI.

INSTRUMENT(S): Synapt G2-S HDMS, nanoACQUITY UPLC

ORGANISM(S): Escherichia Coli (ncbitaxon:562)

SUBMITTER: Elyssia Gallagher

PROVIDER: MSV000091635 | MassIVE | Tue Apr 04 09:26:00 BST 2023

REPOSITORIES: MassIVE

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Gas-phase stability and thermodynamics of ligand-bound, binary complexes of chloramphenicol acetyltransferase reveal negative cooperativity.

Edwards Alexis N AN Blue Anthony J AJ Conforti Jessica M JM Cordes Michael S MS Trakselis Michael A MA Gallagher Elyssia S ES

Analytical and bioanalytical chemistry 20230805 25

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 thermody ...[more]

PMID: 37542535

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