Inhibition of β-lactamases of mycobacteria by avibactam and clavulanate | Zendy

Daria Soroka | Zendy; Clément Ourghanlian | Zendy; Fabrice Compain | Zendy; Marion Fichini | Zendy; Vincent Dubée | Zendy; JeanLuc Mainardi | Zendy; JeanEmmanuel Hugonnet | Zendy; Michel Arthur | Zendy

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Inhibition of β-lactamases of mycobacteria by avibactam and clavulanate

Author(s) -

Daria Soroka,

Clément Ourghanlian,

Fabrice Compain,

Marion Fichini,

Vincent Dubée,

JeanLuc Mainardi,

JeanEmmanuel Hugonnet,

Michel Arthur

Publication year - 2016

Publication title -

journal of antimicrobial chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.124

H-Index - 194

eISSN - 1460-2091

pISSN - 0305-7453

DOI - 10.1093/jac/dkw546

Subject(s) - avibactam , enzyme kinetics , beta lactamase inhibitors , mycobacterium tuberculosis , escherichia coli , microbiology and biotechnology , biology , mycobacterium , clavulanic acid , drug resistance , chemistry , biochemistry , klebsiella pneumoniae , amoxicillin , enzyme , tuberculosis , bacteria , antibiotics , active site , medicine , genetics , pathology , gene

Mycobacterium tuberculosis and Mycobacterium abscessus produce broad-spectrum class A β-lactamases, BlaC and Bla Mab , which are inhibited by clavulanate and avibactam, respectively. BlaC differs from Bla Mab at Ambler position 132 in the conserved motif SDN (SDG versus SDN, respectively). Here, we investigated whether this polymorphism could account for the inhibition specificity of β-lactamases from slowly and rapidly growing mycobacteria.

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