Alcohol dehydrogenase 1 (Saccharomyces cerevisiae) (YADH)

Alcohol dehydrogenase 1 (YADH) from Saccharomyces cerevisiae is a tetrameric, zinc-dependent enzyme that plays a pivotal role in the fermentation process by catalyzing the final step of the glycolytic pathway. It facilitates the reversible reduction of acetaldehyde to ethanol, coupled with the oxidation of NADH to NAD+, which is essential for maintaining the redox balance required for continued anaerobic metabolism [1][5]. While YADH is not a primary therapeutic target for human diseases, it is extensively utilized as a model enzyme in biochemistry and structural biology to understand the mechanism of the broader alcohol dehydrogenase family, including human isoforms [2]. In industrial applications, YADH is critical for the production of bioethanol and serves as a key reagent in clinical diagnostic kits for the quantification of ethanol in blood and other biological samples [4]. Although it is not a standard drug target, research into YADH inhibitors like pyrazole and its derivatives provides a framework for developing antifungal agents, though selectivity remains a challenge due to high structural homology with human ADH [3][5]. The enzyme's dependence on zinc and its specific kinetic properties make it a staple in enzymatic assays and metabolic engineering studies [2][4]. References: [1] UniProtKB - P00330 (ADH1_YEAST). [2] Plapp, B. V. (2010) Adv Enzymol Relat Areas Mol Biol. [3] Raj, S. B., et al. (2014) J Genet Eng Biotechnol. [4] Sigma-Aldrich Product Info. [5] Leskovac, V., et al. (2002) Int J Biochem Cell Biol.

Other names

ADH1YADH-IAlcohol dehydrogenase (yeast)Ethanol dehydrogenase

Inhibitors typically coordinate with the catalytic zinc ion within the active site or compete with the NAD+ cofactor to block the reduction of acetaldehyde to ethanol [2][5].