ArticleProceedings of the National Academy of Sciences of the United States of America2026
Hydration and hydrolysis define antibiotic resistance conferred by macrolide esterases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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7 authors.
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Abstract
Macrolides are an antibiotic class widely used in both human and veterinary medicine, and function by interfering with protein synthesis. Regrettably, numerous strategies for evading the antibiotic properties of macrolides have been found in bacteria, including enzyme-mediated inactivation. These mechanisms are now widely disseminated among pathogenic, animal-associated, and environmental bacteria making them a One Health issue. Macrolide esterases, which hydrolyze the macrolactone's ester bond, confer one such resistance mechanism. Two types of macrolide esterases have thus far been identified, the well-studied erythromycin esterases and the recently discovered Est-type enzymes that belong to the α/β-hydrolase superfamily. We present detailed structure-function studies for four diverse Est type esterases: which only share 44 to 66% sequence identity (EstT
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