Structural Insights into the Mechanism of Carbapenemase Activity of the OXA-48 β-Lactamase-Reference-Cited by-同舟云学术

Structural Insights into the Mechanism of Carbapenemase Activity of the OXA-48 β-Lactamase

Published:2019-10 Issue:10 Volume:63 Page:
ISSN:0066-4804
Container-title:Antimicrobial Agents and Chemotherapy
language:en
Short-container-title:Antimicrob Agents Chemother

Author:

Smith Clyde A.¹,Stewart Nichole K.²,Toth Marta²,Vakulenko Sergei B.²

Affiliation:

1. Stanford Synchrotron Radiation Lightsource, Stanford University, Menlo Park, California, USA

2. Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA

Abstract

Carbapenem-hydrolyzing class D carbapenemases (CHDLs) are enzymes that produce resistance to the last-resort carbapenem antibiotics, severely compromising the available therapeutic options for the treatment of life-threatening infections. A broad variety of CHDLs, including OXA-23, OXA-24/40, and OXA-58, circulate in Acinetobacter baumannii , while the OXA-48 CHDL is predominant in Enterobacteriaceae .

Funder

HHS | NIH | National Institute of Allergy and Infectious Diseases

HHS | NIH | National Institute of General Medical Sciences

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Link

https://journals.asm.org/doi/pdf/10.1128/AAC.01202-19

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1. Carbapenems: Past, Present, and Future

2. Comparative Review of the Carbapenems