Crystallization and preliminary X-ray analysis of the NADPH-dependent 3-quinuclidinone reductase from Rhodotorula rubra

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 65; no. 6; pp. 645 - 647
• Main Authors: Takeshita, Daijiro, Kataoka, Michihiko, Miyakawa, Takuya, Miyazono, Ken-ichi, Uzura, Atsuko, Nagata, Koji, Shimizu, Sakayu, Tanokura, Masaru
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.06.2009
• Subjects: 3-quinuclidinone reductase; Alcohol Oxidoreductases - genetics; Alcohol Oxidoreductases - isolation & purification; Alcohol Oxidoreductases - metabolism; Aldehyde Reductase; Aldo-Keto Reductases; carbonyl reductases; Catalysis; Cloning, Molecular; Crystallization; Crystallization Communications; Crystallography, X-Ray; Data Collection; Escherichia coli; Escherichia coli - genetics; Genetic Vectors; Hydrogen-Ion Concentration; Plasmids; Quinuclidines - isolation & purification; Quinuclidines - metabolism; Rhodotorula - enzymology; Rhodotorula rubra; short-chain dehydrogenase/reductase family; Statistics as Topic; Substrate Specificity; Temperature; Transformation, Bacterial; X-Ray Diffraction

(R)‐3‐Quinuclidinol is a useful compound that is applicable to the synthesis of various pharmaceuticals. The NADPH‐dependent carbonyl reductase 3‐quinuclidinone reductase from Rhodotorula rubra catalyzes the stereospecific reduction of 3‐quinuclidinone to (R)‐3‐quinuclidinol and is expected to be ut...