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LAM-1 from Lysobacter antibioticus: A potent zinc-dependent activity that inactivates ß-lactam antibiotics.
Stroek, Rozanne; Wilson, Liam; Goracke, William; Kang, Taeuk; Vermue, Febe; Krco, Stefan; Mendels, Yonatan; Douw, Andrew; Morris, Marc; Knaven, Esmee G; Mitic, Natasa; Gutierrez, Maria C R; Schenk, Elaine B; Clark, Alice; Garcia, David; Monteiro Pedroso, Marcelo; Schenk, Gerhard.
Afiliação
  • Stroek R; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Wilson L; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Goracke W; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Kang T; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Vermue F; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Krco S; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Mendels Y; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Douw A; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Morris M; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Knaven EG; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Mitic N; Department of Chemistry, Maynooth University, Maynooth, Co. Kildare, Ireland.
  • Gutierrez MCR; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Schenk EB; School of Mathematics and Physics, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Clark A; Sustainable Minerals Institute, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Garcia D; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
  • Monteiro Pedroso M; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia; Sustainable Minerals Institute, The University of Queensland, St. Lucia, Queensland 4072, Australia. Electronic address: m.pedroso@uq.edu.au.
  • Schenk G; School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia; Sustainable Minerals Institute, The University of Queensland, St. Lucia, Queensland 4072, Australia; Australian Institute for Bioengineering and Nanotechnology, The University of Queen
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.
Assuntos

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

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