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Evidence for the dissociation of horse liver alcohol dehydrogenase into subunits in the presence of detergent

1967; Elsevier BV; Volume: 122; Issue: 1 Linguagem: Inglês

10.1016/0003-9861(67)90146-4

1096-0384

Charles H. Blomquist, David A. Smith, Aaron M. Martinez,

Microbial Metabolic Engineering and Bioproduction

This chapter describes the advances with an emphasis on the structures of the alcohol dehydrogenases and the relationship between structure and function. Yeast and mammalian alcohol dehydrogenase differ in substrate specificity and rate of catalytic activity. The classic yeast enzyme is more specific for acetaldehyde and ethanol, which is consistent with its recognized physiological Significance to participate in alcohol fermentation at the end of the glycolytic pathway. Enzyme forms with other functions and properties also occur in yeast. The mammalian enzymes have broad substrate specificity and, even with primary alcohols, the maximum activity is not observed with ethanol. Alcohols including ethanol, produced in the intestinal tracts mainly by bacterial actions, are found in the portal vein. One physiological function of liver alcohol dehydrogenase may be to metabolize these products. Structural studies have established that mammalian alcohol dehydrogenases have a distant evolutionary link to both the yeast and bacterial enzymes. Ingested alcohol is metabolized to acetaldehyde mainly by the action of liver alcohol dehydrogenase.