4185-00-6Relevant articles and documents
Enzymatic α/β Inversion of C-3 Hydroxyl of Bile Acids and Study of the Effects of Organic Solvents on Reaction Rates
Riva, Sergio,Bovara, Roberto,Zetta, Lucia,Pasta, Piero,Ottolina, Gianluca,Carrera, Giacomo
, p. 88 - 92 (1988)
Enzymatic α/β inversion of the C-3 hydroxyl of numerous bile acids containing different numbers of hydroxyl groups in the skeleton and side chains of different lengths has been carried out.Inversion was obtained in two steps through the sequential use of the commercial enzymes 3α- and 3β-hydroxysteroid dehydrogenase, employed in the free form or immobilized on Eupergit C.The transformations were practically quantitative and the products more than 98percent pure.NAD was regenerated in situ with the pyruvate/lactic dehydrogenase system and NADH with the formate/formate dehydrogenase system.The effects of product inhibition on reaction rates and the favorable effects produced by low concentrations (7-10percent, v/v) of ethyl acetate and ethanol were also examined.
Regiospecific oxidoreductions catalyzed by a new Pseudomonas paucimobilis hydroxysteroid dehydrogenase
Bianchini, Ercolina,Chinaglia, Nicola,Dean, Mariangela,Giovannini, Pier Paolo,Medici, Alessandro,Pedrini, Paola,Poli, Silvia
, p. 1391 - 1398 (2007/10/03)
The preparative-scale regio- and stereo-specific oxidation of hydroxy groups and reduction of keto functions at C(3) of several C21 bile acids, catalyzed by a new 3α-hydroxysteroid dehydrogenase (3α-HSDH) is reported. The crude enzyme, isolated from the cells of Pseudomonas paucimobilis, revealed the presence of a further enzymatic fraction containing a secondary alcohol dehydrogenase (SADH), that has been used to recycle the cofactor.
