scholarly journals Back Cover: Deracemization of Secondary Alcohols by using a Single Alcohol Dehydrogenase (ChemCatChem 8/2016)

ChemCatChem ◽  
2016 ◽  
Vol 8 (8) ◽  
pp. 1599-1599 ◽  
Author(s):  
Ibrahim Karume ◽  
Masateru Takahashi ◽  
Samir M. Hamdan ◽  
Musa M. Musa
Keyword(s):  
Alcohol Dehydrogenase ◽  
Secondary Alcohols ◽  
Back Cover

scholarly journals Inside Back Cover: Chemoenzymatic Deracemization of Secondary Alcohols by using a TEMPO-Iodine-Alcohol Dehydrogenase System (ChemCatChem 24/2015)

ChemCatChem ◽  
2015 ◽  
Vol 7 (24) ◽  
pp. 4197-4197
Author(s):  
Daniel Méndez-Sánchez ◽  
Juan Mangas-Sánchez ◽  
Iván Lavandera ◽  
Vicente Gotor ◽  
Vicente Gotor-Fernández
Keyword(s):  
Alcohol Dehydrogenase ◽  
Secondary Alcohols ◽  
Back Cover ◽  
Dehydrogenase System

Deracemization of Secondary Alcohols by using a Single Alcohol Dehydrogenase

ChemCatChem ◽  
2016 ◽  
Vol 8 (8) ◽  
pp. 1459-1463 ◽  
Author(s):  
Ibrahim Karume ◽  
Masateru Takahashi ◽  
Samir M. Hamdan ◽  
Musa M. Musa
Keyword(s):  
Alcohol Dehydrogenase ◽  
Secondary Alcohols

Racemization of enantiopure secondary alcohols by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase

2013 ◽  
Vol 11 (17) ◽  
pp. 2911 ◽  
Author(s):  
Musa M. Musa ◽  
Robert S. Phillips ◽  
Maris Laivenieks ◽  
Claire Vieille ◽  
Masateru Takahashi ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Secondary Alcohol ◽  
Secondary Alcohols ◽  
Thermoanaerobacter Ethanolicus ◽  
Secondary Alcohol Dehydrogenase

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.

scholarly journals Chemoenzymatic Deracemization of Secondary Alcohols by using a TEMPO-Iodine-Alcohol Dehydrogenase System

ChemCatChem ◽  
2015 ◽  
Vol 7 (24) ◽  
pp. 4016-4020 ◽  
Author(s):  
Daniel Méndez-Sánchez ◽  
Juan Mangas-Sánchez ◽  
Iván Lavandera ◽  
Vicente Gotor ◽  
Vicente Gotor-Fernández
Keyword(s):  
Alcohol Dehydrogenase ◽  
Secondary Alcohols ◽  
Dehydrogenase System
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