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- W4284666963 abstract "The abundance of recorded protein sequence data stands in contrast to the small number of experimentally verified functional annotation. Here we screened a million-membered metagenomic library at ultrahigh throughput in microfluidic droplets for β-glucuronidase activity. We identified SN243, a genuine β-glucuronidase with little homology to previously studied enzymes of this type, as a glycoside hydrolase 3 family member. This glycoside hydrolase family contains only one recently added β-glucuronidase, showing that a functional metagenomic approach can shed light on assignments that are currently ‘unpredictable’ by bioinformatics. Kinetic analyses of SN243 characterized it as a promiscuous catalyst and structural analysis suggests regions of divergence from homologous glycoside hydrolase 3 members creating a wide-open active site. With a screening throughput of >107 library members per day, picolitre-volume microfluidic droplets enable functional assignments that complement current enzyme database dictionaries and provide bridgeheads for the annotation of unexplored sequence space. Functional screening of a large metagenomic library with a droplet microfluidics platform enabled the discovery of SN243, a bacterial β-glucuronidase from the glycoside hydrolase 3 family, which was characterized structurally and biochemically." @default.
- W4284666963 created "2022-07-08" @default.
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- W4284666963 date "2022-07-07" @default.
- W4284666963 modified "2023-10-17" @default.
- W4284666963 title "Functional metagenomic screening identifies an unexpected β-glucuronidase" @default.
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- W4284666963 doi "https://doi.org/10.1038/s41589-022-01071-x" @default.
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