US EPA

2346152 

Journal Article 

Reversible oxidation of cyclic secondary alcohols by liver alcohol dehydrogenase 

Merritt, AD; Tomkins, GM 

1959 

Yes 

Journal of Biological Chemistry
ISSN: 0021-9258
EISSN: 1083-351X 

234 

2778-2782 

English 

http://www.jbc.org/content/234/10/2778.citation
Exit
 

During a study of cyclic alcohol oxidation by a partially purified rat liver enzyme system (l), it was noted that ethanol was also oxidized by this preparation. Since the ratio of the rate of ethanol oxidation to the rate of cyclohexanol oxidation remained constant during purification, the possibility arose that the activity with cyclic substrates was due to the conventional alcohol dehydrogenase of liver. To examine this question, crystalline alcohol dehydrogenases from yeast and horse liver
were tested. Cyclic alcohols were inactive with the yeast enzyme but, in the presence of horse liver alcohol dehydrogenase, they caused a rapid reduction of diphosphopyridine nucleotide as follows (2) :

Cyclohexanol + DPN+ <=> cyclohexanone + DPNH + H+

During the course of these studies, Winer (3) reported the occurrence of such a reaction. Some characteristics of this system are presented below.