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
Showing 1 - 4 results of 4 for search 'GALE', query time: 0.09s Refine Results
  1. 1
    by GALE
    Published P.Jaya: Eastern Univ. Press Sdn.Bhd., 1981.
  2. 2
    by GALE
    Published New York: Free Press, 1994.
  3. 3
    by GALE
    Published Singapore: Eastern Universiti Press, 1982.
  4. 4
    Published P.Jaya: Pelanduk Pub., 1986.
    Other Authors: “…Gale,…”