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- W2063755536 abstract "The generation of new enzymatic activities has mainly relied on repurposing the interiors of preexisting protein folds because of the challenge in designing functional, three-dimensional protein structures from first principles. Here we report an artificial metallo-β-lactamase, constructed via the self-assembly of a structurally and functionally unrelated, monomeric redox protein into a tetrameric assembly that possesses catalytic zinc sites in its interfaces. The designed metallo-β-lactamase is functional in the Escherichia coli periplasm and enables the bacteria to survive treatment with ampicillin. In vivo screening of libraries has yielded a variant that displays a catalytic proficiency [(k(cat)/K(m))/k(uncat)] for ampicillin hydrolysis of 2.3 × 10(6) and features the emergence of a highly mobile loop near the active site, a key component of natural β-lactamases to enable substrate interactions." @default.
- W2063755536 created "2016-06-24" @default.
- W2063755536 creator A5039312032 @default.
- W2063755536 creator A5051768466 @default.
- W2063755536 date "2014-12-19" @default.
- W2063755536 modified "2023-10-14" @default.
- W2063755536 title "A designed supramolecular protein assembly with in vivo enzymatic activity" @default.
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- W2063755536 doi "https://doi.org/10.1126/science.1259680" @default.
- W2063755536 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25525249" @default.
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