UDP-galactose 4-epimerase (GALE)

UDP-galactose 4-epimerase (GALE) is an essential enzyme of the Leloir pathway involved in galactose metabolism. It catalyzes the reversible conversion of UDP-galactose and UDP-glucose, as well as UDP-N-acetylgalactosamine and UDP-N-acetylglucosamine, enabling the utilization and biosynthesis of galactose-containing glycans and glycolipids required for proper cellular function[1][2][3][4][5]. GALE is crucial for processes such as glycoprotein and glycolipid formation, cellular signaling, and energy production. Mutations in GALE can result in type III galactosemia, with a spectrum of clinical severity ranging from asymptomatic to life-threatening, depending on residual enzymatic activity and tissue distribution of the deficiency[1][4]. No targeted therapies exist; management is based on dietary modification in severe forms.

Other names

UDP-glucose 4-epimeraseUDP-GalNAc 4-epimeraseUDP-GlcNAc 4-epimeraseSDR1E1GalactowaldenaseUDP-N-acetylgalactosamine 4-epimeraseUDP-N-acetylglucosamine 4-epimeraseshort chain dehydrogenase/reductase family 1E member 1

Inhibitors would reduce enzymatic activity, blocking interconversion of UDP-glucose/galactose and/or UDP-GlcNAc/GalNAc