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- W1955811668 startingPage "4060" @default.
- W1955811668 abstract "As an alternative to Darwinian evolution relying on catalytic promiscuity, a protein may acquire auxiliary function upon metal binding, thus providing it with a novel catalytic machinery. Here we show that addition of cupric ions to a 6-phosphogluconolactonase 6-PGLac bearing a putative metal binding site leads to the emergence of peroxidase activity (kcat 7.8 × 10-2 s-1, KM 1.1 × 10-5 M). Both X-ray crystallographic and EPR data of the copper-loaded enzyme Cu·6-PGLac reveal a bis-histidine coordination site, located within a shallow binding pocket capable of accommodating the o-dianisidine substrate." @default.
- W1955811668 created "2016-06-24" @default.
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- W1955811668 date "2015-01-01" @default.
- W1955811668 modified "2023-10-16" @default.
- W1955811668 title "Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding" @default.
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- W1955811668 doi "https://doi.org/10.1039/c5sc01065a" @default.
- W1955811668 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5707476" @default.
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- W1955811668 hasPublicationYear "2015" @default.
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