{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T02:28:18Z","timestamp":1790908098588,"version":"4.1.0"},"reference-count":47,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2013,4,1]],"date-time":"2013-04-01T00:00:00Z","timestamp":1364774400000},"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":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2013,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            A novel thermostable alcohol dehydrogenase (ADH) showing activity toward aromatic secondary alcohols was identified from the hyperthermophilic archaeon\n            <jats:named-content content-type=\"genus-species\">Thermococcus kodakarensis<\/jats:named-content>\n            KOD1 (\n            <jats:italic>Tk<\/jats:italic>\n            ADH). The gene,\n            <jats:italic>tk0845<\/jats:italic>\n            , which encodes an aldo-keto reductase, was heterologously expressed in\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            . The enzyme was found to be a monomer with a molecular mass of 31 kDa. It was highly thermostable with an optimal temperature of 90\u00ef\u00bf\u00bdC and a half-life of 4.5 h at 95\u00ef\u00bf\u00bdC. The apparent\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            values for the cofactors NAD(P)\n            <jats:sup>+<\/jats:sup>\n            and NADPH were similar within a range of 66 to 127 \u03bcM.\n            <jats:italic>Tk<\/jats:italic>\n            ADH preferred secondary alcohols and accepted various ketones and aldehydes as substrates. Interestingly, the enzyme could oxidize 1-phenylethanol and its derivatives having substituents at the\n            <jats:italic>meta<\/jats:italic>\n            and\n            <jats:italic>para<\/jats:italic>\n            positions with high enantioselectivity, yielding the corresponding (\n            <jats:italic>R<\/jats:italic>\n            )-alcohols with optical purities of greater than 99.8% enantiomeric excess (ee).\n            <jats:italic>Tk<\/jats:italic>\n            ADH could also reduce 2,2,2-trifluoroacetophenone to (\n            <jats:italic>R<\/jats:italic>\n            )-2,2,2-trifluoro-1-phenylethanol with high enantioselectivity (&gt;99.6% ee). Furthermore, the enzyme showed high resistance to organic solvents and was particularly highly active in the presence of H\n            <jats:sub>2<\/jats:sub>\n            O\u201320% 2-propanol and H\n            <jats:sub>2<\/jats:sub>\n            O\u201350%\n            <jats:italic>n<\/jats:italic>\n            -hexane or\n            <jats:italic>n<\/jats:italic>\n            -octane. This ADH is expected to be a useful tool for the production of aromatic chiral alcohols.\n          <\/jats:p>","DOI":"10.1128\/aem.03873-12","type":"journal-article","created":{"date-parts":[[2013,1,26]],"date-time":"2013-01-26T02:32:43Z","timestamp":1359167563000},"page":"2209-2217","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":31,"title":["Thermostable Alcohol Dehydrogenase from Thermococcus kodakarensis KOD1 for Enantioselective Bioconversion of Aromatic Secondary Alcohols"],"prefix":"10.1128","volume":"79","author":[{"given":"Xi","family":"Wu","sequence":"first","affiliation":[{"name":"Department of Chemical Engineering, Tsinghua University, Beijing, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chong","family":"Zhang","sequence":"additional","affiliation":[{"name":"Department of Chemical Engineering, Tsinghua University, Beijing, 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