Stereoselective synthesis of (<Emphasis Type="Italic">R</Emphasis>)-3-quinuclidinol through asymmetric reduction of 3-quinuclidinone with 3-quinuclidinone reductase of <Emphasis Type="Italic">Rhodotorula rubra</Emphasis> |
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Authors: | Atsuko Uzura Fumiki Nomoto Akiko Sakoda Yukifumi Nishimoto Michihiko Kataoka Sakayu Shimizu |
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Institution: | (1) Research & Development Center, Nagase & Co., Ltd., 2-2-3 Murotani, Nishi-ku, Kobe 651-2241, Japan;(2) Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwakecho, Sakyo-ku, Kyoto 606-8502, Japan |
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Abstract: | A novel nicotinamide adenine dinucleotide phosphate-dependent carbonyl reductase, 3-quinuclidinone reductase, was isolated
from Rhodotorula rubra JCM3782. The enzyme catalyzes the asymmetric reduction of 3-quinuclidinone to (R)-3-quinuclidinol. The gene encoding the enzyme was also cloned and sequenced. A 819-bp nucleotide fragment was confirmed
to be the gene encoding the 3-quinuclidinone reductase by agreement of the internal amino acid sequences of the purified enzyme.
The gene encodes a total of 272 amino acid residues, and the deduced amino acid sequence shows similarity to those of several
short-chain dehydrogenase/reductase family proteins. An expression vector, pWKLQ, which contains the full length 3-quinuclidinone
reductase gene was constructed. Using Escherichia coli cells coexpressing the 3-quinuclidinone reductase and glucose dehydrogenase (cofactor regeneration enzyme) genes, 618 mM
3-quinuclidinone was almost stiochiometrically converted to (R)-3-quinuclidinol with an >99.9% enantiomeric excess within 21 h of reaction. |
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Keywords: | 3-Quinuclidinone reductase Rhodotorula rubra Asymmetric reduction (R)-3-Quinuclidinol |
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