{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,17]],"date-time":"2026-09-17T00:34:25Z","timestamp":1789605265465,"version":"build-2803163510"},"reference-count":26,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2012,10,19]],"date-time":"2012-10-19T00:00:00Z","timestamp":1350604800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>We found two NADH-dependent reductases (QNR and bacC) in Microbacterium luteolum JCM 9174 (M. luteolum JCM 9174) that can reduce 3-quinuclidinone to optically pure (R)-(\u2212)-3-quinuclidinol. Alcohol dehydrogenase from Leifsonia sp. (LSADH) was combined with these reductases to regenerate NAD+ to NADH in situ in the presence of 2-propanol as a hydrogen donor. The reductase and LSADH genes were efficiently expressed in E. coli cells. A number of constructed E. coli biocatalysts (intact or immobilized) were applied to the resting cell reaction and optimized. Under the optimized conditions, (R)-(\u2212)-3-quinuclidinol was synthesized from 3-quinuclidinone (15% w\/v, 939 mM) giving a conversion yield of 100% for immobilized QNR. The optical purity of the (R)-(\u2212)-3-quinuclidinol produced by the enzymatic reactions was &gt;99.9%. Thus, E. coli biocatalysis should be useful for the practical production of the pharmaceutically important intermediate, (R)-(\u2212)-3-quinuclidinol.<\/jats:p>","DOI":"10.3390\/ijms131013542","type":"journal-article","created":{"date-parts":[[2012,10,22]],"date-time":"2012-10-22T05:32:03Z","timestamp":1350883923000},"page":"13542-13553","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Production of (R)-3-Quinuclidinol by E. coli Biocatalysts Possessing NADH-Dependent 3-Quinuclidinone Reductase (QNR or bacC) from Microbacterium luteolum and Leifsonia Alcohol Dehydrogenase (LSADH)"],"prefix":"10.3390","volume":"13","author":[{"given":"Kentaro","family":"Isotani","sequence":"first","affiliation":[{"name":"Department of Biotechnology, Faculty of Engineering, Biotechnology Research Center, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Junji","family":"Kurokawa","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Faculty of Engineering, Biotechnology Research Center, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nobuya","family":"Itoh","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Faculty of Engineering, Biotechnology Research Center, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2012,10,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1002\/1521-3773(20010105)40:1<40::AID-ANIE40>3.0.CO;2-5","article-title":"Asymmetric catalysis by architectural and functional molecular engineering: Practical chemo- and stereoselective hydrogenation of ketones","volume":"40","author":"Noyori","year":"2001","journal-title":"Angew. 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