{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T23:37:48Z","timestamp":1790293068866,"version":"4.1.0"},"reference-count":31,"publisher":"Oxford University Press (OUP)","issue":"12","license":[{"start":{"date-parts":[[2024,10,10]],"date-time":"2024-10-10T00:00:00Z","timestamp":1728518400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32302033"],"award-info":[{"award-number":["32302033"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100021171","name":"Guangdong Basic and Applied Basic Research Foundation","doi-asserted-by":"publisher","award":["2022A1515110917"],"award-info":[{"award-number":["2022A1515110917"]}],"id":[{"id":"10.13039\/501100021171","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Guangzhou Basic and Applied Basic Research Foundation","award":["2023A04J1494"],"award-info":[{"award-number":["2023A04J1494"]}]},{"name":"GDAS\u2019 Project of Science and Technology Development","award":["2022GDASZH-2022010110"],"award-info":[{"award-number":["2022GDASZH-2022010110"]}]},{"name":"GDAS\u2019 Project of Science and Technology Development","award":["2023GDASZH-2023010102"],"award-info":[{"award-number":["2023GDASZH-2023010102"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,12,10]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Gut microbes produce \u03b1-l-fucosidases critical for utilizing human milk oligosaccharides, mucosal and dietary glycans. Although gut Parabacteroides have garnered attention for their impact on host health and disease, their CAZymes remain poorly studied. CAZome analysis of eleven gut Parabacteroides type strains revealed their capacity to degrade mucin O-glycans. Their abundance of GH29 fucosidases caught our attention, and we predicted the functional profiles of 46 GH29 fucosidases using in silico approaches. Our findings showed diverse linkages specificities and species-specific distributions, with over half of GH29 enzymes functioning as \u03b11,3\/4 fucosidases, essential for acting on Lewis antigen epitopes of mucin O-glycans. We further enzymatically validated 4 novel GH29 sequences from poorly characterized groups. PgoldGH29A (cluster37GH29BERT, GH29:75.1CUPP) does not act on tested natural substrates. PgoldGH29B (cluster1GH29BERT, GH29:84.1CUPP) functions as a strict \u03b11,3\/4 fucosidase. PgoldGH29C (cluster14GH29BERT, GH29:29.1CUPP) displays unprecedented substrate specificity for \u03b11,2\/3\/4 disaccharides. PgoldGH29D (cluster4GH29BERT, GH29:6.2CUPP) acts on \u03b11,2\/3\/4\/6 linkages similar to enzymes from GH29:6.1CUPP but prefers disaccharides over trisaccharides. These results suggest that PgoldGH29B and PgoldGH29D can contribute to mucin O-glycan degradation via their \u03b11,3\/4 and \u03b11,2 fucosidase activity, respectively, while the natural substrates of PgoldGH29A and PgoldGH29C may be irrelevant to host-glycans. These insights enhance our understanding of the ecological niches inhabited by gut Parabacteroides and may guide similar exploration in other intriguing gut microbial species.<\/jats:p>","DOI":"10.1093\/glycob\/cwae086","type":"journal-article","created":{"date-parts":[[2024,10,10]],"date-time":"2024-10-10T11:34:30Z","timestamp":1728560070000},"source":"Crossref","is-referenced-by-count":5,"title":["Bioinformatics-aided function exploration of GH29 fucosidases from human gut <i>Parabacteroides<\/i>"],"prefix":"10.1093","volume":"34","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6601-4777","authenticated-orcid":false,"given":"Haiyang","family":"Wu","sequence":"first","affiliation":[{"name":"Guangdong Engineering Technology Research Centre of Enzyme and Biocatalysis , Institute of Biological and Medical Engineering, , No. 10 Shiliugang Road, Haizhu District, Guangzhou, Guangdong 510316,","place":["P. R. China"]},{"name":"Guangdong Academy of Sciences , Institute of Biological and Medical Engineering, , No. 10 Shiliugang Road, Haizhu District, Guangzhou, Guangdong 510316,","place":["P. R. China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7460-9546","authenticated-orcid":false,"given":"Qingxin","family":"Li","sequence":"additional","affiliation":[{"name":"Guangdong Engineering Technology Research Centre of Enzyme and Biocatalysis , Institute of Biological and Medical Engineering, , No. 10 Shiliugang Road, Haizhu District, Guangzhou, Guangdong 510316,","place":["P. R. China"]},{"name":"Guangdong Academy of Sciences , Institute of Biological and Medical Engineering, , No. 10 Shiliugang Road, Haizhu District, Guangzhou, Guangdong 510316,","place":["P. R. China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-4693-3174","authenticated-orcid":false,"given":"Jin Chuan","family":"Wu","sequence":"additional","affiliation":[{"name":"Guangdong Engineering Technology Research Centre of Enzyme and Biocatalysis , Institute of Biological and Medical Engineering, , No. 10 Shiliugang Road, Haizhu District, Guangzhou, Guangdong 510316,","place":["P. R. China"]},{"name":"Guangdong Academy of Sciences , Institute of Biological and Medical Engineering, , No. 10 Shiliugang Road, Haizhu District, Guangzhou, Guangdong 510316,","place":["P. R. 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