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- W4372317709 endingPage "1791" @default.
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- W4372317709 abstract "Copper radical oxidases (CROs) are redox enzymes able to oxidize alcohols or aldehydes, while only requiring a single copper atom as cofactor. Studied CROs are found in one of two subfamilies within the Auxiliary Activities family 5 (AA5) in the carbohydrate‐active enzymes database. We here characterize an AA5 enzyme outside the subfamily classification from the opportunistic bacterial pathogen Burkholderia pseudomallei , which curiously was fused to a carbohydrate esterase family 3 domain. The enzyme was shown to be a promiscuous primary alcohol oxidase, with an activity profile similar to enzymes from subfamily 2. The esterase domain was inactive on all tested substrates, and structural predictions revealed this being an effect of crippling substitutions in the expected active site residues." @default.
- W4372317709 created "2023-05-07" @default.
- W4372317709 creator A5012489737 @default.
- W4372317709 creator A5021594300 @default.
- W4372317709 creator A5035184005 @default.
- W4372317709 date "2023-05-11" @default.
- W4372317709 modified "2023-09-26" @default.
- W4372317709 title "A unique <scp>AA5</scp> alcohol oxidase fused with a catalytically inactive <scp>CE3</scp> domain from the bacterium <i>Burkholderia pseudomallei</i>" @default.
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- W4372317709 doi "https://doi.org/10.1002/1873-3468.14632" @default.
- W4372317709 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37143387" @default.
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