GALE:NAD+ dimer reversibly epimerises UDP-Gal to UDP-Glc

Stable Identifier
Reaction [transition]
Homo sapiens
UDP-galactose <=> UDP-glucose
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Cytosolic UDP-galactose 4-epimerase catalyzes the interconversion of UDP-D-galactose and UDP-D-glucose (Schulz et al. 2004). The active form of the enzyme is a homodimer with one molecule of bound NAD+ per monomer (Thoden et al. 2000).

Literature References
PubMed ID Title Journal Year
10801319 Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase

Thoden, JB, Fridovich-Keil, JL, Wohlers, TM, Holden, HM

Biochemistry 2000
15175331 Determinants of function and substrate specificity in human UDP-galactose 4'-epimerase

Schulz, JM, Thoden, JB, Fridovich-Keil, JL, Watson, AL, Ross, KL, Holden, HM, Sanders, R

J Biol Chem 2004
Catalyst Activity

UDP-glucose 4-epimerase activity of GALE:NAD+ dimer [cytosol]

Orthologous Events
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