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The red algal polysaccharide porphyran contains the methoxy sugar 6-<jats:italic>O<\/jats:italic>-methyl-<jats:sc>d<\/jats:sc>-galactose (G6Me). In the degradation of porphyran, oxidative demethylation of this monosaccharide towards <jats:sc>d<\/jats:sc>-galactose and formaldehyde occurs, which is catalyzed by a\u00a0cytochrome P450 monooxygenase and its redox partners. In direct proximity to the genes encoding for the key enzymes of this oxidative demethylation, genes encoding for zinc-dependent alcohol dehydrogenases (ADHs) were identified, which seem to be conserved in porphyran utilizing marine <jats:italic>Flavobacteriia<\/jats:italic>. Considering the fact that dehydrogenases could play an auxiliary role in carbohydrate degradation, we aimed to elucidate the physiological role of these marine ADHs. Although our results reveal that the ADHs are not involved in formaldehyde detoxification, a knockout of the ADH gene causes a dramatic growth defect of <jats:italic>Zobellia galactanivorans<\/jats:italic> with G6Me as a substrate. This indicates that the ADH is required for G6Me utilization. Complete biochemical characterizations of the ADHs from <jats:italic>Formosa agariphila<\/jats:italic> KMM 3901<jats:sup>T<\/jats:sup> (FoADH) and <jats:italic>Z. galactanivorans<\/jats:italic> Dsij<jats:sup>T<\/jats:sup> (ZoADH) were performed, and the substrate screening revealed that these enzymes preferentially convert aromatic aldehydes. Additionally, we elucidated the crystal structures of FoADH and ZoADH in complex with NAD<jats:sup>+<\/jats:sup> and showed that the strict substrate specificity of these new auxiliary enzymes is based on a narrow active site.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Key points<\/jats:title>\n                <jats:p><jats:italic>\u2022 Knockout of the ADH-encoding gene revealed its role in 6-O-methyl-D-galactose utilization, suggesting a new auxiliary activity in marine carbohydrate degradation.<\/jats:italic><\/jats:p>\n                <jats:p><jats:italic>\u2022 Complete enzyme characterization indicated no function in a subsequent reaction of the oxidative demethylation, such as formaldehyde detoxification.<\/jats:italic><\/jats:p>\n                <jats:p><jats:italic>\u2022 These marine ADHs preferentially convert aromatic compounds, and their strict substrate specificity is based on a narrow active site.<\/jats:italic><\/jats:p>\n              <\/jats:sec>","DOI":"10.1007\/s00253-023-12447-x","type":"journal-article","created":{"date-parts":[[2023,3,7]],"date-time":"2023-03-07T10:03:27Z","timestamp":1678183407000},"page":"2363-2384","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Unique alcohol dehydrogenases involved in algal sugar utilization by marine bacteria"],"prefix":"10.1007","volume":"107","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2346-7706","authenticated-orcid":false,"given":"Stefan","family":"Brott","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3268-354X","authenticated-orcid":false,"given":"Ki Hyun","family":"Nam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1896-0774","authenticated-orcid":false,"given":"Fran\u00e7ois","family":"Thomas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3053-9536","authenticated-orcid":false,"given":"Theresa","family":"Dutschei","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8957-4083","authenticated-orcid":false,"given":"Lukas","family":"Reisky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3757-588X","authenticated-orcid":false,"given":"Maike","family":"Behrens","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6352-0212","authenticated-orcid":false,"given":"Hanna C.","family":"Grimm","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3009-6205","authenticated-orcid":false,"given":"Gurvan","family":"Michel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7213-3596","authenticated-orcid":false,"given":"Thomas","family":"Schweder","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0685-2696","authenticated-orcid":false,"given":"Uwe T.","family":"Bornscheuer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2023,3,7]]},"reference":[{"key":"12447_CR1","doi-asserted-by":"publisher","first-page":"2248","DOI":"10.1104\/pp.103.022277","volume":"132","author":"H Achkor","year":"2003","unstructured":"Achkor H, D\u00edaz M, Fern\u00e1ndez MR, Biosca JA, Par\u00e9s X, Mart\u00ednez MC (2003) Enhanced formaldehyde detoxification by overexpression of glutathione-dependent formaldehyde dehydrogenase from Arabidopsis. 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