{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T13:14:06Z","timestamp":1791983646679,"version":"4.4.0"},"reference-count":39,"publisher":"Microbiology Society","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2009,6,1]]},"abstract":"<jats:p>Two alkyl alcohol dehydrogenase (ADH) genes from the long-chain alkane-degrading strain<jats:italic>Geobacillus thermodenitrificans<\/jats:italic>NG80-2 were characterized<jats:italic>in vitro<\/jats:italic>. ADH1 and ADH2 were prepared heterologously in<jats:italic>Escherichia coli<\/jats:italic>as a homooctameric and a homodimeric protein, respectively. Both ADHs can oxidize a broad range of alkyl alcohols up to at least C<jats:sub>30<\/jats:sub>, as well as 1,3-propanediol and acetaldehyde. ADH1 also oxidizes glycerol, and ADH2 oxidizes isopropyl alcohol, isoamylol, acetone, octanal and decanal. The best substrate is ethanol for ADH1 and 1-octanol for ADH2. For both ADHs, the optimum assay condition is at 60\u2005\u00b0C and pH\u20058.0, and both NAD and NADP can be used as the cofactor. Sequence analysis reveals that ADH1 and ADH2 belong to the Fe-containing\/activated long-chain ADHs. However, the two enzymes contain neither Fe nor other metals, and Fe is not required for the activity, suggesting a new type of ADH. The ADHs characterized here are potentially useful in crude oil bioremediation and other bioconversion processes.<\/jats:p>","DOI":"10.1099\/mic.0.027201-0","type":"journal-article","created":{"date-parts":[[2009,6,1]],"date-time":"2009-06-01T18:09:04Z","timestamp":1243879744000},"page":"2078-2085","source":"Crossref","is-referenced-by-count":36,"title":["Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2"],"prefix":"10.1099","volume":"155","author":[{"given":"Xueqian","family":"Liu","sequence":"first","affiliation":[{"name":"Tianjin Research Center for Functional Genomics and Biochip, Tianjin 300457, PR China"},{"name":"Tianjin Key Laboratory of Microbial Functional Genomics, Tianjin 300457, PR China"},{"name":"TEDA School of Biological Sciences and Biotechnology, Nankai University, Tianjin 300457, PR 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binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal Biochem"},{"key":"R5","doi-asserted-by":"crossref","first-page":"2151","DOI":"10.1128\/JB.177.8.2151-2156.1995","article-title":"Purification of 1,3-propanediol dehydrogenase from Citrobacter freundii and cloning, sequencing, and overexpression of the corresponding gene in Escherichia coli","volume":"177","author":"Daniel","year":"1995","journal-title":"J Bacteriol"},{"key":"R6","doi-asserted-by":"crossref","first-page":"5602","DOI":"10.1073\/pnas.0609650104","article-title":"Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir","volume":"104","author":"Feng","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R7","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/1357-2725(95)00138-7","article-title":"Purification and characterization of the alcohol dehydrogenase from a novel strain of Bacillus stearothermophilus growing at 70\u2005\u00b0C","volume":"28","author":"Guagliardi","year":"1996","journal-title":"Int J Biochem Cell Biol"},{"key":"R8","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/S1389-1723(04)70191-7","article-title":"Properties of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix K1","volume":"97","author":"Hirakawa","year":"2004","journal-title":"J Biosci Bioeng"},{"key":"R9","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1016\/S1389-1723(01)80170-5","article-title":"Characterization of the NADH-linked acetylacetoin reductase\/2,3-butanediol dehydrogenase gene from Bacillus cereus YUF-4","volume":"91","author":"Hosaka","year":"2001","journal-title":"J Biosci Bioeng"},{"key":"R10","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1128\/AEM.46.1.98-105.1983","article-title":"Thermostable NAD-linked secondary alcohol dehydrogenase from propane-grown Pseudomonas fluorescens NRRL B-1244","volume":"46","author":"Hou","year":"1983","journal-title":"Appl Environ Microbiol"},{"key":"R11","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1007\/s00792-006-0034-1","article-title":"A cold-active and thermostable alcohol dehydrogenase of a psychrotorelant from Antarctic seawater, Flavobacterium frigidimaris KUC-1","volume":"11","author":"Kazuoka","year":"2007","journal-title":"Extremophiles"},{"key":"R12","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"R13","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1128\/JB.144.2.569-578.1980","article-title":"Ethanol production by thermophilic bacteria: relationship between fermentation product yields of and catabolic enzyme activities in Clostridium thermocellum and Thermoanaerobium brockii","volume":"144","author":"Lamed","year":"1980","journal-title":"J Bacteriol"},{"issue":"144","key":"R14","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S0009-2797(02)00166-7","article-title":"Properties and functional significance of Saccharomyces cerevisiae ADHVI","volume":"143","author":"Larroy","year":"2003","journal-title":"Chem Biol Interact"},{"key":"R15","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1111\/j.1574-6968.1997.tb12665.x","article-title":"Glycerol conversion to 1,3-propanediol by Clostridium pasteurianum : cloning and expression of the gene encoding 1,3-propanediol dehydrogenase","volume":"154","author":"Luers","year":"1997","journal-title":"FEMS Microbiol Lett"},{"key":"R16","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1128\/JB.181.4.1163-1170.1999","article-title":"An unusual oxygen-sensitive, iron- and zinc-containing alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus 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III dehydrogenase that interconverts l-lactaldehyde and l-1,2-propanediol in Escherichia coli","volume":"187","author":"Montella","year":"2005","journal-title":"J Bacteriol"},{"key":"R20","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1111\/j.1432-1033.1986.tb09366.x","article-title":"The two alcohol dehydrogenases of Zymomonas mobilis . Purification by differential dye ligand chromatography, molecular characterisation and physiological roles","volume":"154","author":"Neale","year":"1986","journal-title":"Eur J Biochem"},{"key":"R21","doi-asserted-by":"crossref","first-page":"3949","DOI":"10.1128\/AEM.00217-08","article-title":"Purification and characterization of a novel recombinant highly enantioselective short-chain NAD(H)-dependent alcohol dehydrogenase from Thermus thermophilus","volume":"74","author":"Pennacchio","year":"2008","journal-title":"Appl Environ Microbiol"},{"key":"R22","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/S0168-6445(03)00068-8","article-title":"Alcohol dehydrogenases from thermophilic and hyperthermophilic archaea and bacteria","volume":"27","author":"Radianingtyas","year":"2003","journal-title":"FEMS Microbiol Rev"},{"key":"R23","doi-asserted-by":"crossref","first-page":"13","DOI":"10.3109\/10408419409113545","article-title":"Molecular characterization of microbial alcohol dehydrogenases","volume":"20","author":"Reid","year":"1994","journal-title":"Crit Rev Microbiol"},{"key":"R24","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1016\/S0969-2126(01)00645-1","article-title":"Glycerol dehydrogenase: structure, specificity, and mechanism of a family III polyol dehydrogenase","volume":"9","author":"Ruzheinikov","year":"2001","journal-title":"Structure"},{"key":"R25","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1002\/prot.10594","article-title":"Crystal structure of an iron-containing 1,3-propanediol dehydrogenase (TM0920) from Thermotoga maritima at 1.3\u200aA\u030a resolution","volume":"54","author":"Schwarzenbacher","year":"2004","journal-title":"Proteins"},{"key":"R26","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/0014-5793(83)80517-1","article-title":"An iron-activated alcohol dehydrogenase","volume":"156","author":"Scopes","year":"1983","journal-title":"FEBS Lett"},{"key":"R27","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/343038a0","article-title":"Redesign of the coenzyme specificity of a dehydrogenase by protein engineering","volume":"343","author":"Scrutton","year":"1990","journal-title":"Nature"},{"key":"R28","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1128\/JB.164.3.1017-1024.1985","article-title":"Alcohol dehydrogenases in Acinetobacter sp. strain HO1-N: role in hexadecane and hexadecanol metabolism","volume":"164","author":"Singer","year":"1985","journal-title":"J Bacteriol"},{"key":"R29","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1016\/j.jmb.2004.07.034","article-title":"Crystal structure of E. coli alcohol dehydrogenase YqhD: evidence of a covalently modified NADP coenzyme","volume":"342","author":"Sulzenbacher","year":"2004","journal-title":"J Mol Biol"},{"key":"R30","doi-asserted-by":"crossref","first-page":"5231","DOI":"10.1128\/AEM.66.12.5231-5235.2000","article-title":"Thermostable NADP+-dependent medium-chain alcohol dehydrogenase from Acinetobacter sp. strain M-1: purification and characterization and gene expression in Escherichia coli","volume":"66","author":"Tani","year":"2000","journal-title":"Appl Environ Microbiol"},{"key":"R31","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/0003-2697(76)90558-3","article-title":"A microgel system for disc electrophoresis","volume":"72","author":"Tulchin","year":"1976","journal-title":"Anal Biochem"},{"key":"R32","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1099\/00221287-147-3-745","article-title":"An inducible 1-butanol dehydrogenase, a quinohaemoprotein, is involved in the oxidation of butane by \u2018 Pseudomonas butanovora \u2019","volume":"147","author":"Vangnai","year":"2001","journal-title":"Microbiology"},{"key":"R33","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/S0031-9422(02)00560-5","article-title":"Homologous very-long-chain 1,3-alkanediols and 3-hydroxyaldehydes in leaf cuticular waxes of Ricinus communis L","volume":"62","author":"Vermeer","year":"2003","journal-title":"Phytochemistry"},{"key":"R34","doi-asserted-by":"crossref","first-page":"3949","DOI":"10.1016\/S0021-9258(19)67885-3","article-title":"Electron microscopic analysis and biochemical characterization of a novel methanol dehydrogenase from the thermotolerant Bacillus sp","volume":"266","author":"Vonck","year":"1991","journal-title":"C1. J Biol Chem"},{"key":"R35","doi-asserted-by":"crossref","first-page":"7149","DOI":"10.1128\/JB.174.22.7149-7158.1992","article-title":"Molecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes","volume":"174","author":"Walter","year":"1992","journal-title":"J Bacteriol"},{"key":"R36","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1007\/s00792-006-0505-4","article-title":"Isolation and characterization of a novel thermophilic Bacillus strain degrading long-chain n-alkanes","volume":"10","author":"Wang","year":"2006","journal-title":"Extremophiles"},{"key":"R37","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1007\/s00253-007-1119-1","article-title":"Bacterial metabolism of long-chain n-alkanes","volume":"76","author":"Wentzel","year":"2007","journal-title":"Appl Microbiol Biotechnol"},{"key":"R38","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.1021\/bi00327a012","article-title":"Interaction of pyrophosphate moieties with alpha-helixes in dinucleotide binding proteins","volume":"24","author":"Wierenga","year":"1985","journal-title":"Biochemistry"},{"key":"R39","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1007\/s00203-007-0217-x","article-title":"Purification and characterization of an iron-containing alcohol dehydrogenase in extremely thermophilic bacterium Thermotoga hypogea","volume":"187","author":"Ying","year":"2007","journal-title":"Arch Microbiol"}],"container-title":["Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/micro\/10.1099\/mic.0.027201-0?crawler=true","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,10,6]],"date-time":"2021-10-06T16:12:00Z","timestamp":1633536720000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/micro\/10.1099\/mic.0.027201-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,6,1]]},"references-count":39,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2009,6,1]]}},"URL":"https:\/\/doi.org\/10.1099\/mic.0.027201-0","relation":{},"ISSN":["1350-0872","1465-2080"],"issn-type":[{"value":"1350-0872","type":"print"},{"value":"1465-2080","type":"electronic"}],"subject":[],"published":{"date-parts":[[2009,6,1]]}}}