A unique AA5 alcohol oxidase fused with a catalytically inactive CE3 domain from the bacterium Burkholderia pseudomallei
Artikel i vetenskaplig tidskrift, 2023

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.

Auxiliary Activity family 5

alcohol oxidase

Burkholderia

copper-radical oxidase

multidomain enzyme

Författare

Scott Mazurkewich

Chalmers, Life sciences, Industriell bioteknik

Andrea Seveso

Chalmers, Life sciences, Industriell bioteknik

Johan Larsbrink

Chalmers, Life sciences, Industriell bioteknik

FEBS Letters

0014-5793 (ISSN) 18733468 (eISSN)

Vol. 597 13 1779-1791

Ämneskategorier

Biokemi och molekylärbiologi

Strukturbiologi

DOI

10.1002/1873-3468.14632

PubMed

37143387

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Senast uppdaterat

2023-07-24