UDP-glucose 4-epimerase
The enzyme UDP-glucose 4-epimerase (), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.Additionally, human and some bacterial GALE isoforms reversibly catalyze the formation of UDP-''N''-acetylgalactosamine (UDP-GalNAc) from UDP-''N''-acetylglucosamine (UDP-GlcNAc) in the presence of NAD+, an initial step in glycoprotein or glycolipid synthesis. Provided by Wikipedia
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11Published 1984Other Authors: “…Gale…”
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19Published 1987Other Authors: “…edited byMarc L.Miller,Richard P.Gale and Perry.J.Brown…”