| Function
UDP-galactose 4-epimerase (GalE) reversibly converts UDP-galactose to UDP-glucose. GalE catalyzes the last step in galactose metabolism[1]. GalE uses NAD+ as a cofactor.
Disease
Mutations in GalE are the cause of galactosemia which is autosomal recessive disorder[2].
Structural highlights
GalE active site contains the substrate UDP-galactose (UDP-gal) and the cofactor NAD. Water molecules are shown as red spheres. Tyrosine residue is the catalytic base which produces the ketose intermediate[3].
- ↑ Mozzi F, Savoy de Giori G, Font de Valdez G. UDP-galactose 4-epimerase: a key enzyme in exopolysaccharide formation by Lactobacillus casei CRL 87 in controlled pH batch cultures. J Appl Microbiol. 2003;94(2):175-83. PMID:12534808
- ↑ Park HD, Park KU, Kim JQ, Shin CH, Yang SW, Lee DH, Song YH, Song J. The molecular basis of UDP-galactose-4-epimerase (GALE) deficiency galactosemia in Korean patients. Genet Med. 2005 Nov-Dec;7(9):646-9. PMID:16301867 doi:10.109701.gim.0000194023.27802.2d
- ↑ Alphey MS, Burton A, Urbaniak MD, Boons GJ, Ferguson MA, Hunter WN. Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):829-34. Epub 2006 Aug 11. PMID:16946458 doi:10.1107/S1744309106028740
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3D structures of UDP-galactose 4 epimerase
UDP-galactose 4-epimerase 3D structures
References
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