{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T07:19:34Z","timestamp":1790666374879,"version":"4.1.0"},"reference-count":33,"publisher":"American Society for Microbiology","issue":"8","license":[{"start":{"date-parts":[[2013,4,15]],"date-time":"2013-04-15T00:00:00Z","timestamp":1365984000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2013,4,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            A putative maltose\/maltodextrin operon was found in the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Sulfolobus acidocaldarius<\/jats:named-content>\n            DSM639 genome. The gene cluster consisted of 7 genes (\n            <jats:italic>malA<\/jats:italic>\n            ,\n            <jats:italic>trmB<\/jats:italic>\n            ,\n            <jats:italic>amyA<\/jats:italic>\n            ,\n            <jats:italic>malG<\/jats:italic>\n            ,\n            <jats:italic>malF<\/jats:italic>\n            ,\n            <jats:italic>malE<\/jats:italic>\n            , and\n            <jats:italic>malK<\/jats:italic>\n            ). Here, we report the identification of MalA, which is responsible for the hydrolysis of maltose or maltodextrin to glucose in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">S. acidocaldarius<\/jats:named-content>\n            . The transcription level of\n            <jats:italic>malA<\/jats:italic>\n            was increased 3-fold upon the addition of maltose or starch to the medium. Moreover, the \u03b1-glucosidase activity for maltose as a substrate in cell extracts of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">S. acidocaldarius<\/jats:named-content>\n            DSM639 was also 11- and 10-fold higher during growth in YT medium (Brock's mineral salts, 0.1% [wt\/vol] tryptone, and 0.005% [wt\/vol] yeast extract) containing maltose or starch, respectively, than during growth on other sugars. The gene encoding MalA was cloned and expressed in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">S. acidocaldarius<\/jats:named-content>\n            . The enzyme purified from the organism was a dodecamer in its active state and showed strong maltose-hydrolyzing activity at 100\u00b0C and pH 5.0. MalA was remarkably thermostable, with half-lives of 33.8 h, 10.6 h, and 1.8 h at 95\u00b0C, 100\u00b0C, and 105\u00b0C, respectively. Substrate specificity and kinetic studies of MalA with maltooligosaccharides indicated that MalA efficiently hydrolyzed maltose to maltopentaose, which is a typical characteristic of GH31-type \u03b1-glucosidases. However, glycogen or starch was not hydrolyzed. Reverse transcription-PCR, sugar uptake, and growth studies of the wild-type DSM639 and \u0394\n            <jats:italic>malEFG<\/jats:italic>\n            mutant on different sugars demonstrated that MalA located in the\n            <jats:italic>mal<\/jats:italic>\n            operon gene cluster is involved in maltose and starch metabolism in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">S. acidocaldarius<\/jats:named-content>\n            .\n          <\/jats:p>","DOI":"10.1128\/jb.01713-12","type":"journal-article","created":{"date-parts":[[2013,2,9]],"date-time":"2013-02-09T03:55:40Z","timestamp":1360382140000},"page":"1789-1799","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":23,"title":["Identification and Characterization of MalA in the Maltose\/Maltodextrin Operon of Sulfolobus acidocaldarius DSM639"],"prefix":"10.1128","volume":"195","author":[{"given":"Kyoung-Hwa","family":"Choi","sequence":"first","affiliation":[{"name":"Department of Microbiology, College of Natural Sciences, Pusan National University, Busan, South Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sungmin","family":"Hwang","sequence":"additional","affiliation":[{"name":"Department of Microbiology, College of Natural Sciences, Pusan National University, Busan, South Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jaeho","family":"Cha","sequence":"additional","affiliation":[{"name":"Department of Microbiology, College of Natural Sciences, Pusan National University, Busan, South Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1007\/s00203-008-0392-4","article-title":"Genetic tools for Sulfolobus spp.: vectors and first applications","volume":"190","author":"Berkner S","year":"2008","unstructured":"BerknerS LippsG. 2008. 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