A comprehensive investigation of the anion inhibition profile of a ß-carbonic anhydrase from Acinetobacter baumannii for crafting innovative antimicrobial treatments.
J Enzyme Inhib Med Chem
; 39(1): 2372731, 2024 Dec.
Article
em En
| MEDLINE
| ID: mdl-39012078
ABSTRACT
This study refers to the intricate world of Acinetobacter baumannii, a resilient pathogenic bacterium notorious for its propensity at antibiotic resistance in nosocomial infections. Expanding upon previous findings that emphasised the bifunctional enzyme PaaY, revealing unexpected γ-carbonic anhydrase (CA) activity, our research focuses on a different class of CA identified within the A. baumannii genome, the ß-CA, designated as ð½-AbauCA (also indicated as CanB), which plays a crucial role in the resistance mechanism mediated by AmpC beta-lactamase. Here, we cloned, expressed, and purified the recombinant ð½-AbauCA, unveiling its distinctive kinetic properties and inhibition profile with inorganic anions (classical CA inhibitors). The exploration of ð½-AbauCA not only enhances our understanding of the CA repertoire of A. baumannii but also establishes a foundation for targeted therapeutic interventions against this resilient pathogen, promising advancements in combating its adaptability and antibiotic resistance.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Inibidores da Anidrase Carbônica
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Testes de Sensibilidade Microbiana
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Anidrases Carbônicas
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Acinetobacter baumannii
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Ânions
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Antibacterianos
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article