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
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

243-281

Informations de copyright

Copyright © 2024. Published by Elsevier Inc.

Auteurs

Molly S Youse (MS)

Borch Department of Medicinal Chemistry and Molecular Pharmacology, College of Pharmacy, Purdue University, West Lafayette, IN, United States.

Katrina J Holly (KJ)

Borch Department of Medicinal Chemistry and Molecular Pharmacology, College of Pharmacy, Purdue University, West Lafayette, IN, United States.

Daniel P Flaherty (DP)

Borch Department of Medicinal Chemistry and Molecular Pharmacology, College of Pharmacy, Purdue University, West Lafayette, IN, United States. Electronic address: dflaher@purdue.edu.

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Classifications MeSH