Neisseria gonorrhoeae carbonic anhydrase inhibition.
Antibiotics
Bacterial carbonic anhydrases
Carbonic anhydrase inhibitors
Neisseria gonorrhoeae
Structure-activity relationship
Journal
The Enzymes
ISSN: 0423-2607
Titre abrégé: Enzymes
Pays: United States
ID NLM: 101637215
Informations de publication
Date de publication:
2024
2024
Historique:
medline:
3
9
2024
pubmed:
3
9
2024
entrez:
2
9
2024
Statut:
ppublish
Résumé
Carbonic anhydrases (CAs) are ubiquitous enzymes that are found in all kingdoms of life. Though different classes of CAs vary in their roles and structures, their primary function is to catalyze the reaction between carbon dioxide and water to produce bicarbonate and a proton. Neisseria gonorrhoeae encodes for three distinct CAs (NgCAs) from three different families: an α-, a β-, and a γ-isoform. This chapter details the differences between the three NgCAs, summarizing their subcellular locations, roles, essentiality, structures, and enzyme kinetics. These bacterial enzymes have the potential to be drug targets; thus, previous studies have investigated the inhibition of NgCAs-primarily the α-isoform. Therefore, the classes of inhibitors that have been shown to bind to the NgCAs will be discussed as well. These classes include traditional CA inhibitors, such as sulfonamides, phenols, and coumarins, as well as non-traditional inhibitors including anions and thiocarbamates.
Identifiants
pubmed: 39222993
pii: S1874-6047(24)00008-8
doi: 10.1016/bs.enz.2024.05.008
pii:
doi:
Substances chimiques
Carbonic Anhydrase Inhibitors
0
Carbonic Anhydrases
EC 4.2.1.1
Bacterial Proteins
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
243-281Informations de copyright
Copyright © 2024. Published by Elsevier Inc.