The preparative-scale regio- and stereo-specific oxidation of hydroxy groups and reduction of keto functions at C(3) of several C24 bile acids catalyzed by a new 3a-hydroxysteroid dehydrogenase (3a-HDH) is reported. The crude enzyme isolated from the cells of Pseudomonas paucimobilis revelead the presence of a further enzymatic fraction containing a secondary alcohol dehydrogenase (SADH) that has been used to recycle the cofactor.
Regiospecific oxidoreductions catalyzed by a new Pseudomonas paucimobilis hydroxysteroid dehydrogenase
BIANCHINI, Ercolina;GIOVANNINI, Pier Paolo;MEDICI, Alessandro;PEDRINI, Paola;
1999
Abstract
The preparative-scale regio- and stereo-specific oxidation of hydroxy groups and reduction of keto functions at C(3) of several C24 bile acids catalyzed by a new 3a-hydroxysteroid dehydrogenase (3a-HDH) is reported. The crude enzyme isolated from the cells of Pseudomonas paucimobilis revelead the presence of a further enzymatic fraction containing a secondary alcohol dehydrogenase (SADH) that has been used to recycle the cofactor.File in questo prodotto:
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