Structural and biochemical characterization of VIM ‐26 shows that Leu224 has implications for the substrate specificity of VIM metallo‐β‐lactamases-Reference-Cited by-同舟云学术

Structural and biochemical characterization of VIM ‐26 shows that Leu224 has implications for the substrate specificity of VIM metallo‐β‐lactamases

Published:2015-02-06 Issue:6 Volume:282 Page:1031-1042
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:The FEBS Journal

Author:

Leiros Hanna‐Kirsti S.¹,Edvardsen Kine Susann Waade¹,Bjerga Gro Elin Kjæreng¹,Samuelsen Ørjan²

Affiliation:

1. Norwegian Structural Biology Centre Department of Chemistry UiT The Arctic University of Norway Tromsø Norway

2. Norwegian National Advisory Unit on Detection of Antimicrobial Resistance Department of Microbiology and Infection Control University Hospital of North Norway Tromsø Norway

Funder

Norwegian Structural Biology Centre

Research Council of Norway

FRIMEDBIO

Tromsø Research Foundation

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.13200

Reference40 articles.

1. WHO(2014)World Health Organization: Antimicrobial resistance: globalreport on surveillance ISBN‐978‐992‐974‐156474‐156478.

2. Metallo-β-lactamase structure and function

3. “Stormy waters ahead”: global emergence of carbapenemases

4. Metallo-β-Lactamases: the Quiet before the Storm?

5. VIM-19, a Metallo-β-Lactamase with Increased Carbapenemase Activity from Escherichia coli and Klebsiella pneumoniae

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