{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T03:13:44Z","timestamp":1771038824246,"version":"3.50.1"},"reference-count":30,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2008,4,1]],"date-time":"2008-04-01T00:00:00Z","timestamp":1207008000000},"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":[[2008,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Trehalose supports the growth of\n            <jats:italic>Thermus thermophilus<\/jats:italic>\n            strain HB27, but the absence of obvious genes for the hydrolysis of this disaccharide in the genome led us to search for enzymes for such a purpose. We expressed a putative \u03b1-glucosidase gene (TTC0107), characterized the recombinant enzyme, and found that the preferred substrate was \u03b1,\u03b1-1,1-trehalose, a new feature among \u03b1-glucosidases. The enzyme could also hydrolyze the disaccharides kojibiose and sucrose (\u03b1-1,2 linkage), nigerose and turanose (\u03b1-1,3), leucrose (\u03b1-1,5), isomaltose and palatinose (\u03b1-1,6), and maltose (\u03b1-1,4) to a lesser extent. Trehalose was not, however, a substrate for the highly homologous \u03b1-glucosidase from\n            <jats:italic>T. thermophilus<\/jats:italic>\n            strain GK24. The reciprocal replacement of a peptide containing eight amino acids in the \u03b1-glucosidases from strains HB27 (LGEHNLPP) and GK24 (EPTAYHTL) reduced the ability of the former to hydrolyze trehalose and provided trehalose-hydrolytic activity to the latter, showing that LGEHNLPP is necessary for trehalose recognition. Furthermore, disruption of the \u03b1-glucosidase gene significantly affected the growth of\n            <jats:italic>T. thermophilus<\/jats:italic>\n            HB27 in minimal medium supplemented with trehalose, isomaltose, sucrose, or palatinose, to a lesser extent with maltose, but not with cellobiose (not a substrate for the \u03b1-glucosidase), indicating that the \u03b1-glucosidase is important for the assimilation of those four disaccharides but that it is also implicated in maltose catabolism.\n          <\/jats:p>","DOI":"10.1128\/jb.01794-07","type":"journal-article","created":{"date-parts":[[2008,1,26]],"date-time":"2008-01-26T01:54:16Z","timestamp":1201312456000},"page":"2298-2305","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":19,"title":["Molecular and Physiological Role of the Trehalose-Hydrolyzing \u03b1-Glucosidase from\n            <i>Thermus thermophilus<\/i>\n            HB27"],"prefix":"10.1128","volume":"190","author":[{"given":"Susana","family":"Alarico","sequence":"first","affiliation":[{"name":"Centro de Neurocie\u0302ncias e Biologia Celular, Departamento de Zoologia, Universidade de Coimbra, 3004-517 Coimbra, Portugal"}]},{"given":"Milton S.","family":"da Costa","sequence":"additional","affiliation":[{"name":"Departamento de Bioqui\u0301mica, Universidade de Coimbra, 3001-401 Coimbra, Portugal"}]},{"given":"Nuno","family":"Empadinhas","sequence":"additional","affiliation":[{"name":"Centro de Neurocie\u0302ncias e Biologia Celular, Departamento de Zoologia, Universidade de Coimbra, 3004-517 Coimbra, Portugal"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1007\/s00792-007-0106-x","volume":"11","year":"2007","unstructured":"Alarico, S., N. Empadinhas, A. Mingote, C. Sim\u00f5es, M. S. Santos, and M. S. da Costa. 2007. Mannosylglycerate is essential for osmotic adjustment in Thermus thermophilus strains HB27 and RQ-1. Extremophiles 11 : 833-840.","journal-title":"Extremophiles"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.71.5.2460-2466.2005"},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1111\/j.1432-1033.1996.0150u.x","volume":"239","year":"1996","unstructured":"Boeck, B., and R. Schinzel. 1996. Purification and characterization of an alpha-glucan phosphorylase from the thermophilic bacterium Thermus thermophilus. Eur. J. Biochem. 239 : 150-155.","journal-title":"Eur. J. 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