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Local interactions with the Glu166 base and the conformation of an active site loop play key roles in carbapenem hydrolysis by the KPC-2 ß-lactamase.
Furey, Ian M; Mehta, Shrenik C; Sankaran, Banumathi; Hu, Liya; Prasad, B V Venkataram; Palzkill, Timothy.
Affiliation
  • Furey IM; Department of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, Texas, USA.
  • Mehta SC; Department of Pharmacology and Chemical 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.
  • Hu L; Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston Texas, USA.
  • Prasad BVV; Department of Biochemistry and Molecular Biology, 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. Electronic address: timothyp@bcm.edu.
J Biol Chem ; 296: 100799, 2021.
Article in En | MEDLINE | ID: mdl-34022225
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Beta-Lactamases / Carbapenems / Klebsiella pneumoniae / Anti-Bacterial Agents Limits: Humans Language: En Journal: J Biol Chem Year: 2021 Type: Article Affiliation country: United States
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Beta-Lactamases / Carbapenems / Klebsiella pneumoniae / Anti-Bacterial Agents Limits: Humans Language: En Journal: J Biol Chem Year: 2021 Type: Article Affiliation country: United States