{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T10:34:23Z","timestamp":1768559663758,"version":"3.49.0"},"reference-count":22,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2024,6,28]],"date-time":"2024-06-28T00:00:00Z","timestamp":1719532800000},"content-version":"vor","delay-in-days":27,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["mLife"],"published-print":{"date-parts":[[2024,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:italic>Hyperthermus butylicus<\/jats:italic> is a hyperthermophilic crenarchaeon that produces 1\u2010butanol as an end product. A thermostable alcohol dehydrogenase (ADH) must be present in <jats:italic>H. butylicus<\/jats:italic> to act as the key enzyme responsible for this production; however, the gene that encodes the ADH has not yet been identified. A novel ADH, HbADH2, was purified from a cell\u2010free extract of <jats:italic>H. butylicus<\/jats:italic>, and its characteristics were determined. The gene that encodes HbADH2 was demonstrated to be <jats:italic>HBUT_RS04850<\/jats:italic> and annotated as a hypothetical protein in <jats:italic>H. butylicus<\/jats:italic>. HbADH2 was found to be a primary\u2013secondary ADH capable of using a wide range of substrates, including butyraldehyde and butanol. Butyraldehyde had the highest specificity constant, calculated as <jats:italic>k<\/jats:italic><jats:sub>c<\/jats:sub><jats:sub>at<\/jats:sub>\/<jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub>, with <jats:italic>k<\/jats:italic><jats:sub>cat<\/jats:sub> and apparent <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> values of 8.00\u2009\u00b1\u20090.22\u2009s<jats:sup>\u22121<\/jats:sup> and 0.59\u2009\u00b1\u20090.07\u2009mM, respectively. The apparent <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> values for other substrates, including ethanol, 1\u2010propanol, 2\u2010propanol, butanol, acetaldehyde, propanal, and acetone, were 4.36\u2009\u00b1\u20090.42, 4.69\u2009\u00b1\u20090.41, 3.74\u2009\u00b1\u20090.46, 2.44\u2009\u00b1\u20090.30, 1.27\u2009\u00b1\u20090.18, 1.55\u2009\u00b1\u20090.20, and 0.68\u2009\u00b1\u20090.04\u2009mM, respectively. The optimal pH values for catalyzing aldehyde reduction and alcohol oxidation were 6.0 and 9.0, respectively, while the optimal temperature was higher than 90\u00b0C due to the increase in enzymatic activity from 60\u00b0C to 90\u00b0C. Based on its substrate specificity, enzyme kinetics, and thermostability, HbADH2 may be the ADH that catalyzes the production of 1\u2010butanol in <jats:italic>H. butylicus<\/jats:italic>. The putative conserved motif sites for NAD(P)<jats:sup>+<\/jats:sup> and iron binding were identified by aligning HbADH2 with previously characterized Fe\u2010containing ADHs.<\/jats:p>","DOI":"10.1002\/mlf2.12126","type":"journal-article","created":{"date-parts":[[2024,6,28]],"date-time":"2024-06-28T08:07:37Z","timestamp":1719562057000},"page":"317-325","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["A novel alcohol dehydrogenase in the hyperthermophilic crenarchaeon <i>Hyperthermus butylicus<\/i>"],"prefix":"10.1002","volume":"3","author":[{"given":"Ching","family":"Tse","sequence":"first","affiliation":[{"name":"Department of Biology University of Waterloo Waterloo Ontario Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6249-9298","authenticated-orcid":false,"given":"Kesen","family":"Ma","sequence":"additional","affiliation":[{"name":"Department of Biology University of Waterloo Waterloo Ontario Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2024,6,28]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"publisher","DOI":"10.1128\/jb.172.7.3959-3965.1990"},{"key":"e_1_2_10_3_1","doi-asserted-by":"publisher","DOI":"10.1155\/2007\/745987"},{"key":"e_1_2_10_4_1","doi-asserted-by":"publisher","DOI":"10.1002\/bit.260280507"},{"key":"e_1_2_10_5_1","doi-asserted-by":"publisher","DOI":"10.1051\/lait:1997325"},{"key":"e_1_2_10_6_1","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.65.11.4973-4980.1999"},{"key":"e_1_2_10_7_1","doi-asserted-by":"publisher","DOI":"10.21767\/2576-1412.100018"},{"key":"e_1_2_10_8_1","doi-asserted-by":"publisher","DOI":"10.21775\/9781910190135.06"},{"key":"e_1_2_10_9_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.181.4.1163-1170.1999"},{"key":"e_1_2_10_10_1","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.72.1.233-238.2006"},{"key":"e_1_2_10_11_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00164a031"},{"key":"e_1_2_10_12_1","doi-asserted-by":"publisher","DOI":"10.1021\/pr070232y"},{"key":"e_1_2_10_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(01)31056-X"},{"key":"e_1_2_10_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0168-6445(03)00068-8"},{"key":"e_1_2_10_15_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkab1112"},{"key":"e_1_2_10_16_1","doi-asserted-by":"publisher","DOI":"10.1128\/br.40.1.42-54.1976"},{"key":"e_1_2_10_17_1","doi-asserted-by":"publisher","DOI":"10.1023\/A:1002001919720"},{"key":"e_1_2_10_18_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.187.14.4957-4966.2005"},{"key":"e_1_2_10_19_1","doi-asserted-by":"publisher","DOI":"10.1128\/mr.43.2.260-296.1979"},{"key":"e_1_2_10_20_1","doi-asserted-by":"publisher","DOI":"10.1093\/clinchem\/22.2.151"},{"key":"e_1_2_10_21_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2007.00901.x"},{"key":"e_1_2_10_22_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gky427"},{"key":"e_1_2_10_23_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"}],"container-title":["mLife"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/mlf2.12126","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,7,23]],"date-time":"2024-07-23T03:44:17Z","timestamp":1721706257000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/mlf2.12126"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,6]]},"references-count":22,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2024,6]]}},"alternative-id":["10.1002\/mlf2.12126"],"URL":"https:\/\/doi.org\/10.1002\/mlf2.12126","archive":["Portico"],"relation":{},"ISSN":["2097-1699","2770-100X"],"issn-type":[{"value":"2097-1699","type":"print"},{"value":"2770-100X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,6]]},"assertion":[{"value":"2023-11-16","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2024-03-19","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2024-06-28","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}