Reduction of organic compounds with thiourea dioxide. I. reduction of ketones to secondary alcohols

1972 ◽  
Vol 13 (5) ◽  
pp. 343-346 ◽  
Author(s):  
Kunio Nakagawa ◽  
Kyoji Minami
Keyword(s):  
Organic Compounds ◽  
Secondary Alcohols ◽  
Thiourea Dioxide ◽  
Reduction Of Ketones

scholarly journals Production and Characterization of a Thermostable Alcohol Dehydrogenase That Belongs to the Aldo-Keto Reductase Superfamily

2006 ◽  
Vol 72 (1) ◽  
pp. 233-238 ◽  
Author(s):  
Ronnie Machielsen ◽  
Agustinus R. Uria ◽  
Servé W. M. Kengen ◽  
John van der Oost
Keyword(s):  
Alcohol Dehydrogenase ◽  
Pyrococcus Furiosus ◽  
Enantiomeric Excess ◽  
Physiological Role ◽  
Secondary Alcohols ◽  
Gene Encoding ◽  
Ph Optimum ◽  
Reduction Of Ketones

ABSTRACT The gene encoding a novel alcohol dehydrogenase that belongs to the aldo-keto reductase superfamily has been identified in the hyperthermophilic archaeon Pyrococcus furiosus. The gene, referred to as adhD, was functionally expressed in Escherichia coli and subsequently purified to homogeneity. The enzyme has a monomeric conformation with a molecular mass of 32 kDa. The catalytic activity of the enzyme increases up to 100°C, and a half-life value of 130 min at this temperature indicates its high thermostability. AdhD exhibits a broad substrate specificity with, in general, a preference for the reduction of ketones (pH optimum, 6.1) and the oxidation of secondary alcohols (pH optimum, 8.8). Maximal specific activities were detected with 2,3-butanediol (108.3 U/mg) and diacetyl-acetoin (22.5 U/mg) in the oxidative and reductive reactions, respectively. Gas chromatrography analysis indicated that AdhD produced mainly (S)-2-pentanol (enantiomeric excess, 89%) when 2-pentanone was used as substrate. The physiological role of AdhD is discussed.

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