{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,5,13]],"date-time":"2025-05-13T15:52:20Z","timestamp":1747151540416,"version":"3.40.5"},"reference-count":32,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2021,11,19]],"date-time":"2021-11-19T00:00:00Z","timestamp":1637280000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM134643","R35"],"award-info":[{"award-number":["GM134643","R35"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2021,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:italic>N<\/jats:italic>\u2010acetylated sugars are often found, for example, on the lipopolysaccharides of Gram\u2010negative bacteria, on the S\u2010layers of Gram\u2010positive bacteria, and on the capsular polysaccharides. Key enzymes involved in their biosynthesis are the sugar <jats:italic>N<\/jats:italic>\u2010acetyltransferases. Here, we describe a structural and functional analysis of one such enzyme from <jats:italic>Helicobacter pullorum<\/jats:italic>, an emerging pathogen that may be associated with gastroenteritis and gallbladder and liver diseases. For this analysis, the gene <jats:italic>BA919\u2010RS02330<\/jats:italic> putatively encoding an <jats:italic>N<\/jats:italic>\u2010acetyltransferase was cloned, and the corresponding protein was expressed and purified. A kinetic analysis demonstrated that the enzyme utilizes dTDP\u20103\u2010amino\u20103,6\u2010dideoxy\u2010<jats:sc>d<\/jats:sc>\u2010glucose as a substrate as well as dTDP\u20103\u2010amino\u20103,6\u2010dideoxy\u2010<jats:sc>d<\/jats:sc>\u2010galactose, albeit at a reduced rate. In addition to this kinetic analysis, a similar enzyme from <jats:italic>Helicobacter bilis<\/jats:italic> was cloned and expressed, and its kinetic parameters were determined. Seven X\u2010ray crystallographic structures of various complexes of the <jats:italic>H. pullorum<\/jats:italic> wild\u2010type enzyme (or the C80T variant) were determined to resolutions of 1.7\u00a0\u00c5 or higher. The overall molecular architecture of the <jats:italic>H. pullorum N\u2010<\/jats:italic>acetyltransferase places it into the Class II left\u2010handed\u2010\u03b2\u2010helix superfamily (L\u03b2H). Taken together, the data presented herein suggest that 3\u2010acetamido\u20103,6\u2010dideoxy\u2010<jats:sc>d<\/jats:sc>\u2010glucose (or the galactose derivative) is found on either the <jats:italic>H. pullorum<\/jats:italic> O\u2010antigen or in another of its complex glycoconjugates. A BLAST search suggests that more than 50 non\u2010pylori <jats:italic>Helicobacter<\/jats:italic> spp. have genes encoding <jats:italic>N<\/jats:italic>\u2010acetyltransferases. Given that there is little information concerning the complex glycans in non\u2010pylori <jats:italic>Helicobacter<\/jats:italic> spp. and considering their zoonotic potential, our results provide new biochemical insight into these pathogens<\/jats:p>","DOI":"10.1002\/pro.4207","type":"journal-article","created":{"date-parts":[[2021,10,15]],"date-time":"2021-10-15T20:17:45Z","timestamp":1634329065000},"page":"2418-2432","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Biochemical investigation of an <scp><i>N<\/i>\u2010<\/scp>acetyltransferase from <scp><i>Helicobacter pullorum<\/i><\/scp>"],"prefix":"10.1002","volume":"30","author":[{"given":"William A.","family":"Griffiths","sequence":"first","affiliation":[{"name":"Department of Biochemistry University of Wisconsin  Madison Wisconsin USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Keelan 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