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Carbonic anhydrases in bacterial pathogens.
Braga, Reygan E; Najar, Fares Z; Murphy, Chelsea L; Patrauchan, Marianna A.
Afiliação
  • Braga RE; Department of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK, United States.
  • Najar FZ; Bioinformatics Core, Oklahoma State University, Stillwater, OK, United States.
  • Murphy CL; Bioinformatics Core, Oklahoma State University, Stillwater, OK, United States.
  • Patrauchan MA; Department of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK, United States. Electronic address: m.patrauchan@okstate.edu.
Enzymes ; 55: 313-342, 2024.
Article em En | MEDLINE | ID: mdl-39222996
ABSTRACT
Carbonic anhydrases (CAs) catalyze the reversable hydration of carbon dioxide to bicarbonate placing them into the core of the biochemical carbon cycle. Due to the fundamental importance of their function, they evolved independently into eight classes, three of which have been recently discovered. Most research on CAs has focused on their representatives in eukaryotic organisms, while prokaryotic CAs received significantly less attention. Nevertheless, prokaryotic CAs play a key role in the fundamental ability of the biosphere to acquire CO2 for photosynthesis and to decompose the organic matter back to CO2. They also contribute to a broad spectrum of processes in pathogenic bacteria, enhancing their ability to survive in a host and, therefore, present a promising target for developing antimicrobials. This review focuses on the distribution of CAs among bacterial pathogens and their importance in bacterial virulence and host-pathogen interactions.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bactérias / Anidrases Carbônicas Limite: Humans Idioma: En Revista: Enzymes Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Estados Unidos País de publicação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bactérias / Anidrases Carbônicas Limite: Humans Idioma: En Revista: Enzymes Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Estados Unidos País de publicação: Estados Unidos