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- W2004424871 abstract "ABSTRACT The catalytic base in family 48 glycosyl hydrolases has not been previously established experimentally. Based on structural and modeling data published to date, we used site-directed mutagenesis and azide rescue activity assays to show definitively that the catalytic base in Thermobifida fusca Cel48A is aspartic acid 225. Of the tested mutants, only Cel48A with the D225E mutation retained partial activity on soluble and insoluble substrates. In azide rescue experiments, only the D225G mutation, in the smallest residue tested, showed an increase in activity with added azide." @default.
- W2004424871 created "2016-06-24" @default.
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- W2004424871 date "2011-09-01" @default.
- W2004424871 modified "2023-10-11" @default.
- W2004424871 title "Determination of the Catalytic Base in Family 48 Glycosyl Hydrolases" @default.
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- W2004424871 doi "https://doi.org/10.1128/aem.05532-11" @default.
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