The focus of the present article, the ADH1B gene, encodes the beta subunit of class I ADH. The functional enzyme consists of homo- and heterodimers of alpha, beta, and gamma subunits; the corresponding genes (ADH1A, ADH1B, and ADH1C) map to chromosome 4q23 together with the other human ADH genes (ADH4, ADH5, ADH6, and ADH7). The clones of the full-length cDNA coding for class I ADH subunits were identified by Ikuta and colleagues, providing the first information regarding their molecular structures [Ikuta and others 1985]. However, studies of ADH began many years before: an ADH protein was firstly purified from Saccharomyces cerevisiae in 1937 [Negelein and Wulff 1937]. Initially, this enzyme attracted interest focused on the need to understand the ability of different organisms to oxidize alcohol [Lutwak-Mann 1938]. Later, numerous molecular studies investigated the role of ADH in a wide range of situations, including alcohol metabolism, human behavior, liver function, and human evolution [Brooks and Zakhari 2014; Buhler and others 2015; Carr and others 2002; Edenberg 2000; Edenberg 2007; Li and others 2011a; Li and others 2011b]. In recent years,
