UDP-glucose-4-epimerase

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UDP-glucose-4-epimerase
UDP-glucose-4-epimerase
UDP-glucose-4-epimerase dimer (human) according to PDB  1EK5

Existing structural data: s. UniProt

Properties of human protein
Mass / length primary structure 348 amino acids
Secondary to quaternary structure Homodimer
Cofactor NAD +
Identifier
Gene name GAEL
External IDs
Enzyme classification
EC, category 5.1.3.2 ,  isomerase
Response type Rearrangement
Substrate UDP-galactose, UDP- N -acetylgalactosamine
Products UDP-glucose, UDP- N -acetylglucosamine
Occurrence
Homology family NAD-dependent epimerase
Parent taxon Creature
Orthologue
human House mouse
Entrez 2582 74246
Ensemble ENSG00000117308 ENSMUSG00000028671
UniProt Q14376 Q8R059
Refseq (mRNA) NM_000403 NM_178389
Refseq (protein) NP_000394 NP_848476
Gene locus Chr 1: 23.8 - 23.8 Mb Chr 4: 135.96 - 135.97 Mb
PubMed search 2582 74246

UDP-glucose 4-epimerase ( gene : GALE ), and UDP-galactose-4-epimerase , is the enzyme that the rearrangement of UDP-galactose to UDP-glucose and vice versa catalyzed . This reaction is a partial step in the utilization of galactose in many living things. Mutations in the GALE gene can lead to epimerase deficiency, which leads to type 3 galactosemia .

Catalyzed equilibrium

UDP-Glu    UDP Gal

UDP-glucose is rearranged to UDP-galactose and vice versa. UDP- N -acetylglucosamine and -galactosamine are accepted as alternative substrates , but these are of no importance for the metabolism as a whole.

Web links

Wikibooks: Biochemistry and Pathobiochemistry: Galactose Metabolism  - Learning and Teaching Materials

Individual evidence

  1. ↑ UniProt Q14376
  2. ↑ Schulz JM, Ross KL, Malmstrom K, Krieger M, Fridovich-Keil JL: Mediators of galactose sensitivity in UDP-galactose 4'-epimerase-impaired mammalian cells . In: J. Biol. Chem. . 280, No. 14, April 2005, pp. 13493-502. doi : 10.1074 / jbc.M414045200 . PMID 15701638 .