Precambrian-Based β-Lactamases: Heat-Stable, “Promiscuous”

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Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian β-lactamases.

We report a sequence reconstruction analysis targeting several Precambrian nodes in the evolution of class-A β-lactamases and the preparation and experimental characterization of their encoded proteins. Despite extensive sequence differences with the modern enzymes (~100 amino acid differences), the proteins resurrected in the laboratory properly fold into the canonical lactamase structure. The...

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From the Department of Infectious Diseases, Lahey Clinic, Burlington, Mass., and Harvard Medical School, Boston (G.A.J.); and the Department of Geographic Medicine and Infectious Diseases, Tufts–New England Medical Center and Tufts University School of Medicine, Boston (L.S.M.-P.). Address reprint requests to Dr. Jacoby at Lahey Clinic, 41 Mall Rd., Burlington, MA 01805, or at george.a.jacoby@l...

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ژورنال

عنوان ژورنال: Microbe Magazine

سال: 2013

ISSN: 1558-7452,1558-7460

DOI: 10.1128/microbe.8.237.1