Abstract
Alcohol dehydrogenase (E.C. 1.1.1.1. ADH) catalyzes the inter-conversion of an alcohol and an aldehyde with NAD+ as a cofactor. In most higher organisms that have been studied, several different isozymes of ADH are present. The main function of these isozymes is presumed to be catabolic, to degrade various alcohols or sterols. This presumption is based primarily on the substrate preferences of the various isozymes and the absence of a fermentative pathway for alcohol production during glycolysis. In many organisms there is a distinctive tissue specificity in the distribution of different ADH isozymes.
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Young, T. et al. (1982). The Alcohol Dehydrogenase Genes of the Yeast, Saccharomyces Cerevisiae: Isolation, Structure, and Regulation. In: Hollaender, A., DeMoss, R.D., Kaplan, S., Konisky, J., Savage, D., Wolfe, R.S. (eds) Genetic Engineering of Microorganisms for Chemicals. Basic Life Sciences. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4142-0_26
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DOI: https://doi.org/10.1007/978-1-4684-4142-0_26
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