A drug-resistant ß-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency.

Soeung, Victoria; Lu, Shuo; Hu, Liya; Judge, Allison; Sankaran, Banumathi; Prasad, B V Venkataram; Palzkill, Timothy

Soeung, Victoria; Lu, Shuo; Hu, Liya; Judge, Allison; Sankaran, Banumathi; Prasad, B V Venkataram; Palzkill, Timothy.

Afiliação

Soeung V; Department of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, Texas, USA.
Lu S; Department of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, Texas, USA.
Hu L; Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, USA.
Judge A; Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, USA.
Sankaran B; Department of Molecular Biophysics and Integrated Bioimaging, Berkeley Center for Structural Biology, Lawrence Berkeley National Laboratory, Berkeley, California, USA.
Prasad BVV; Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, USA; Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA.
Palzkill T; Department of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, Texas, USA; Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, USA; Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA. Ele

J Biol Chem ; 295(52): 18239-18255, 2020 12 25.

Article em En | MEDLINE | ID: mdl-33109613

Assuntos

Antibacterianos/farmacologia; Mutação; Prótons; Resistência beta-Lactâmica/genética; Inibidores de beta-Lactamases/farmacologia; beta-Lactamases/química; beta-Lactamases/metabolismo; Domínio Catalítico; Escherichia coli/enzimologia; Escherichia coli/crescimento & desenvolvimento; Mutagênese Sítio-Dirigida; Conformação Proteica; Especificidade por Substrato; beta-Lactamases/genética

Palavras-chave

antibiotic resistance; antibiotics; beta-lactamase; enzyme inhibitor; enzyme kinetics; enzyme structure

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Prótons / Beta-Lactamases / Resistência beta-Lactâmica / Inibidores de beta-Lactamases / Antibacterianos / Mutação Idioma: En Revista: J Biol Chem Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Estados Unidos

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