{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T14:51:10Z","timestamp":1791298270747,"version":"4.1.0"},"reference-count":35,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2006,10,15]]},"abstract":"<jats:p>Group A streptococcus (Streptococcus pyogenes) is the causative agent of severe invasive infections such as necrotizing fasciitis (the so-called \u2018flesh eating disease\u2019) and toxic-shock syndrome. Spy1600, a glycoside hydrolase from family 84 of the large superfamily of glycoside hydrolases, has been proposed to be a virulence factor. In the present study we show that Spy1600 has no activity toward galactosaminides or hyaluronan, but does remove \u03b2-O-linked N-acetylglucosamine from mammalian glycoproteins \u2013 an observation consistent with the inclusion of eukaryotic O-glycoprotein 2-acetamido-2-deoxy-\u03b2-D-glucopyranosidases within glycoside hydrolase family 84. Proton NMR studies, structure\u2013reactivity studies for a series of fluorinated analogues and analysis of 1,2-dideoxy-2\u2032-methyl-\u03b1-D-glucopyranoso-[2,1-d]-\u03942\u2032-thiazoline as a competitive inhibitor reveals that Spy1600 uses a double-displacement mechanism involving substrate-assisted catalysis. Family 84 glycoside hydrolases are therefore comprised of both prokaryotic and eukaryotic \u03b2-N-acetylglucosaminidases using a conserved catalytic mechanism involving substrate-assisted catalysis. Since these enzymes do not have detectable hyaluronidase activity, many family 84 glycoside hydrolases are most likely incorrectly annotated as hyaluronidases.<\/jats:p>","DOI":"10.1042\/bj20060307","type":"journal-article","created":{"date-parts":[[2006,10,2]],"date-time":"2006-10-02T14:23:22Z","timestamp":1159799002000},"page":"241-247","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a \u03b2-<i>N<\/i>-acetylglucosaminidase and not a hyaluronidase"],"prefix":"10.1042","volume":"399","author":[{"given":"William\u00a0L.","family":"Sheldon","sequence":"first","affiliation":[{"name":"Biomolecular and Biomedical Research Centre, School of Applied Sciences, Northumbria University, Newcastle upon Tyne NE1 8ST, U.K."},{"name":"School of Health, Natural and Social Sciences, University of Sunderland, Sunderland SR1 3SD, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew\u00a0S.","family":"Macauley","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Simon Fraser University, Burnaby, BC, Canada V5A 1S6"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward\u00a0J.","family":"Taylor","sequence":"additional","affiliation":[{"name":"York Structural Biology Laboratory, Department of Chemistry, University of York, York YO31 5YW, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charlotte\u00a0E.","family":"Robinson","sequence":"additional","affiliation":[{"name":"Biomolecular and Biomedical Research Centre, School of Applied Sciences, Northumbria University, Newcastle upon Tyne NE1 8ST, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simon\u00a0J.","family":"Charnock","sequence":"additional","affiliation":[{"name":"Biomolecular and Biomedical Research Centre, School of Applied Sciences, Northumbria University, Newcastle upon Tyne NE1 8ST, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gideon\u00a0J.","family":"Davies","sequence":"additional","affiliation":[{"name":"York Structural Biology Laboratory, Department of Chemistry, University of York, York YO31 5YW, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David\u00a0J.","family":"Vocadlo","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Simon Fraser University, Burnaby, BC, Canada V5A 1S6"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gary\u00a0W.","family":"Black","sequence":"additional","affiliation":[{"name":"Biomolecular and Biomedical Research Centre, School of Applied Sciences, Northumbria University, Newcastle upon Tyne NE1 8ST, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2006,9,27]]},"reference":[{"key":"2021112217500532800_B1","unstructured":"Coutinho\n              P.\u00a0M.\n            \n            \n              Henrissat\n              B.\n            \n          \n          1999\n          Carbohydrate-Active Enzymes server at URL: http:\/\/afmb.cnrs-mrs.fr\/CAZY\/"},{"key":"2021112217500532800_B2","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1093\/hmg\/7.12.1859","article-title":"Novel immunogenic antigen homologous to hyaluronidase in meningioma","volume":"7","author":"Heckel","year":"1998","journal-title":"Hum. 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