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

Clyde A. Smith | Zendy; Nichole K. Stewart | Zendy; Márta Tóth | Zendy; Sergei B. Vakulenko | Zendy

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

Author(s) -

Clyde A. Smith,

Nichole K. Stewart,

Márta Tóth,

Sergei B. Vakulenko

Publication year - 2019

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.01202-19

Subject(s) - mechanism (biology) , computational biology , microbiology and biotechnology , biology , epistemology , philosophy

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 inAcinetobacter baumannii , while the OXA-48 CHDL is predominant inEnterobacteriaceae .

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