ADH3 plays an important role in systemic ethanol metabolism at higher levels of blood ethanol through activation by cytoplasmic solution hydrophobicity
adhA transcription is induced by ethanol or n-propanol, adhA transcription is subject to glucose catabolite repression. Accordingly, both induction of AdhA activity and ethanol utilization are detected only after depletion of glucose
among all tested classes of ADH isoenzymes, only class I has higher activity in serum of patients with breast cancer in stage IV. The total ADH activity is not significantly higher in patients with breast cancer than in healthy controls. The changes in activity, especially in class I ADH, appear to be caused by isoenzymes being released from the organ damaged by metastatic disease
the total ADH activity is significantly higher (44%) among patients with cancer than healthy ones. The activity of class I ADH isoenzymes is elevated only in the serum of patients with metastatic liver cancer. This increase of activity seems to be caused by the enzyme released from liver cancer cells and primary tumors originating in other organs
during the biological aging of sherry wines, where Saccharomyces bayanus has to grow on ethanol owing to the absence of glucose, this isoenzyme plays a prominent role by converting the ethanol into acetaldehyde and producing NADH in the process. Overexpression of the gene ADH2 (from Saccharomyces cerevisiae) during alcoholic fermentation has no effect on the proteomic profile or the net production of some metabolites associated with glycolysis and alcoholic fermentation such as ethanol, acetaldehyde, and glycerol. However, it affects indirectly glucose and ammonium uptakes, cell growth, and intracellular redox potential, which lead to an altered metabolome
the activities of total alcohol dehydrogenase, aldehyde dehydrogenase and class I alcohol dehydrogenase isoenzyme between cancer liver tissues and healthy hepatocytes might be a factor in ethanol metabolism disorders which can intensify carcinogenesis
the changes in the carbon metabolism-associated proteins reflect altered patterns of carbon flux in response to changes in ADH activity in transformed plant leaves
the activities of total alcohol dehydrogenase, aldehyde dehydrogenase and class I alcohol dehydrogenase isoenzyme between cancer liver tissues and healthy hepatocytes might be a factor in ethanol metabolism disorders which can intensify carcinogenesis
females show 70% higher hepatic alcohol dehydrogenase activity and display 60% lower voluntary ethanol intake than males. Following ethanol administration (1 g/kg ip), females generate a transient blood acetaldehyde increase with levels that are 2.5fold greater than in males. Castration of males leads to an increase alcohol dehydrogenase activity the appearance of an acetaldehyde burst a reduction of voluntary ethanol intake comparable with that of females
total activity of alcohol dehydrogenase is not significantly different in cancer and normal cells. The differences between enzymes of drinkers and nondrinkers in both cancer and healthy tissue are not significant
no expression of ADH5 in lung, epididymis, uterus, ovary, thymus, adrenal, small intestine, heart, eye, muscle, brain, testis, stomach, spleen, and liver