LAM-1 from Lysobacter antibioticus: A potent zinc-dependent activity that inactivates ß-lactam antibiotics.
J Inorg Biochem
; 226: 111637, 2022 01.
Article
em En
| MEDLINE
| ID: mdl-34749064
ABSTRACT
Resistance to ß-lactam antibiotics, including the "last-resort" carbapenems, has emerged as a major threat to global health. A major resistance mechanism employed by pathogens involves the use of metallo-ß-lactamases (MBLs), zinc-dependent enzymes that inactivate most of the ß-lactam antibiotics used to treat infections. Variants of MBLs are frequently discovered in clinical environments. However, an increasing number of such enzymes have been identified in microorganisms that are less impacted by human activities. Here, an MBL from Lysobacter antibioticus, isolated from the rhizosphere, has been shown to be highly active toward numerous ß-lactam antibiotics. Its activity is higher than that of some of the most effective MBLs linked to hospital-acquired antibiotic resistance and thus poses an interesting system to investigate evolutionary pressures that drive the emergence of such biocatalysts.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Zinco
/
Beta-Lactamases
/
Beta-Lactamas
/
Lysobacter
/
Antibacterianos
Idioma:
En
Revista:
J Inorg Biochem
Ano de publicação:
2022
Tipo de documento:
Article
País de afiliação:
Austrália