GALE Human

GALE is a homodimeric enzyme, meaning it consists of two identical subunits. The enzyme’s active site binds to the UDP-sugar substrates and facilitates the epimerization reaction through a mechanism involving the transient reduction of the sugar moiety . This reaction is essential for maintaining the balance of UDP-sugar pools, which are necessary for the glycosylation of proteins and lipids .

Mutations in the GALE gene can lead to a genetic disorder known as epimerase deficiency galactosemia (type III galactosemia) . This disorder is characterized by an inability to properly metabolize galactose, leading to the accumulation of toxic metabolites. Symptoms of epimerase deficiency galactosemia can range from mild to severe and may include liver dysfunction, cataracts, and developmental delays .

The recombinant form of UDP-Galactose-4-Epimerase is produced using genetic engineering techniques. The human GALE gene is cloned into an expression vector, which is then introduced into a suitable host organism, such as Escherichia coli or Saccharomyces cerevisiae . The host cells are cultured under conditions that promote the expression of the recombinant enzyme, which is subsequently purified using chromatographic techniques .

Recombinant UDP-Galactose-4-Epimerase has several applications in research and biotechnology. It is used to study the biochemical and structural properties of the enzyme, as well as its role in galactose metabolism and glycosylation . Additionally, the enzyme can be employed as a biocatalyst for the synthesis of various UDP-sugars, which are valuable substrates for glycosylation reactions in the production of glycoproteins and glycolipids .