Unexpected N-acetylation of capreomycin by mycobacterial Eis enzymes | Zendy

Jacob L. Houghton | Zendy; Keith Green | Zendy; Rachel Pricer | Zendy; Abdelrahman S. Mayhoub | Zendy; Sylvie GarneauTsodikova | Zendy

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Unexpected N-acetylation of capreomycin by mycobacterial Eis enzymes

Author(s) -

Jacob L. Houghton,

Keith Green,

Rachel Pricer,

Abdelrahman S. Mayhoub,

Sylvie GarneauTsodikova

Publication year - 2012

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/dks497

Subject(s) - capreomycin , mycobacterium tuberculosis , lysine , acetylation , acetyltransferase , mycobacterium smegmatis , biochemistry , chemistry , microbiology and biotechnology , ethambutol , biology , tuberculosis , medicine , amino acid , antibiotics , streptomycin , pathology , gene

The enhanced intracellular survival (Eis) protein from Mycobacterium tuberculosis (Eis_Mtb), a regio-versatile N-acetyltransferase active towards many aminoglycosides (AGs), confers resistance to kanamycin A in some cases of extensively drug-resistant tuberculosis (XDR-TB). We assessed the activity of Eis_Mtb and of its homologue from Mycobacterium smegmatis (Eis_Msm) against a panel of anti-tuberculosis (TB) drugs and lysine-containing compounds.

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