{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T12:32:08Z","timestamp":1790512328579,"version":"4.1.0"},"reference-count":34,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2007,10,23]],"date-time":"2007-10-23T00:00:00Z","timestamp":1193097600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2008,4]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    YesT, a putative protein from\n                    <jats:italic>Bacillus subtilis<\/jats:italic>\n                    ATCC 6633 that has been provisionally classified as a rhamnogalacturonan acetyl esterase (RGAE) in CE\u201012 family, was cloned, expressed in\n                    <jats:italic>Escherichia<\/jats:italic>\n                    <jats:italic>coli<\/jats:italic>\n                    Rosetta (DE3), and purified. The enzyme is monomeric with a molecular mass of 37 kDa and presents thermophilic properties similar to RGAE from\n                    <jats:italic>Aspergillus aculeatus<\/jats:italic>\n                    , although YesT is more alkaliphilic. The study of inhibitors confirmed the importance of the His and the nucleophilic Ser for the esterase activity, apart from the Asp from the catalytic triad. This enzyme also presents broad substrate specificity, and is active toward 7\u2010aminocephalosporanic acid, cephalosporin C,\n                    <jats:italic>p<\/jats:italic>\n                    \u2010nitrophenyl acetate, \u03b2\u2010naphthyl acetate, glucose pentaacetate, and acetylated xylan. Moreover, YesT achieves a synergistic effect together with xylanase A toward acetylated xylan. As a member of the SGNH family, it does not adopt the common \u03b1\/\u03b2 hydrolase fold. The primary sequence analysis and multiple sequence alignment revealed the lack of a two \u03b2\u2010stranded antiparallel sheet, which results in a clear change in the structure together with the disappearance of one of the three 3\n                    <jats:sub>10<\/jats:sub>\n                    \u2010helices presented in RGAE structure. The similarities found in this article among the topological diagrams of RGAE, YesT, and Esterase A from\n                    <jats:italic>Streptomyces scabies<\/jats:italic>\n                    , Platelet\u2010Activating Factor AcetylHydrolase, isoform Ib, alpha subunit [PAF\u2010AH(Ib)\u03b1\n                    <jats:sub>1<\/jats:sub>\n                    ], PAF\u2010AH(Ib)\u03b1\n                    <jats:sub>2<\/jats:sub>\n                    , the esterase domain from hemagglutinin esterase fusion glycoprotein (HEF1) from Influenza C virus, the thioesterase I (TAP) from\n                    <jats:italic>E. coli<\/jats:italic>\n                    , the hypothetical protein a1r1529 from\n                    <jats:italic>Nostoc<\/jats:italic>\n                    sp., and the hypothetical YxiM precursor that all belong to the SGNH family could indicate a possible divergence of such proteins from a common ancestor. Proteins 2008. \u00a9 2007 Wiley\u2010Liss, Inc.\n                  <\/jats:p>","DOI":"10.1002\/prot.21705","type":"journal-article","created":{"date-parts":[[2007,10,23]],"date-time":"2007-10-23T14:45:45Z","timestamp":1193150745000},"page":"379-388","source":"Crossref","is-referenced-by-count":28,"title":["YesT: A new rhamnogalacturonan acetyl esterase from\n                    <i>Bacillus subtilis<\/i>"],"prefix":"10.1002","volume":"71","author":[{"given":"Irene","family":"Mart\u00ednez\u2010Mart\u00ednez","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos\u00e9","family":"Navarro\u2010Fern\u00e1ndez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos\u00e9","family":"Daniel Lozada\u2010Ram\u00edrez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francisco","family":"Garc\u00eda\u2010Carmona","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00c1lvaro","family":"S\u00e1nchez\u2010Ferrer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2007,10,23]]},"reference":[{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1104\/pp.113.4.1265"},{"key":"e_1_2_7_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(97)00209-8"},{"key":"e_1_2_7_4_2","first-page":"3","volume-title":"Recent advances in carbohydrate bioengineering","author":"Coutinho P","year":"1999"},{"key":"e_1_2_7_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(00)00118-0"},{"key":"e_1_2_7_6_2","doi-asserted-by":"publisher","DOI":"10.1099\/00221287-143-8-2605"},{"key":"e_1_2_7_7_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.270.45.27172"},{"key":"e_1_2_7_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(88)60168-6"},{"key":"e_1_2_7_9_2","volume-title":"Molecular cloning: a laboratory manual","author":"Sambrook J","year":"1989"},{"key":"e_1_2_7_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(72)26003-7"},{"key":"e_1_2_7_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(85)81343-0"},{"key":"e_1_2_7_12_2","unstructured":"S\u00e1nchez\u2010FerrerA Mart\u00ednez\u2010Mart\u00ednezI Garc\u00eda\u2010PizarroE Garc\u00eda\u2010CarmonaF. 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