UDP-galactopyranose mutase
UDP-galactopyranose mutase tetramer, Aspergillus fumigatus
Identifiers
EC no.	5.4.99.9
CAS no.	174632-18-9
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, an UDP-galactopyranose mutase (EC 5.4.99.9) is an enzyme that catalyzes the chemical reaction

UDP-D-galactopyranose ${\displaystyle \rightleftharpoons }$ UDP-D-galacto-1,4-furanose

Hence, this enzyme has one substrate, UDP-D-galactopyranose, and one product, UDP-D-galacto-1,4-furanose.

This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is UDP-D-galactopyranose furanomutase.

UDP-D-galactofuranose then serves as an activated sugar donor for the biosynthesis of galactofuranose glycoconjugates. The exocyclic 1,2-diol of galactofuranose is the epitope recognized by the putative chordate immune lectin intelectin.

Structural studies

Because UGM is not present in the mammalian systems but is essential among several pathogenic microbes, the enzyme is an attractive antibiotic target. As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1I8T, 1V0J, 1WAM, 2BI7, and 2BI8.

References

• Trejo AG, Chittenden GJ, Buchanan JG, Baddiley J (1970). "Uridine diphosphate alpha-D-galactofuranose, an intermediate in the biosynthesis of galactofuranosyl residues". Biochem. J. 117 (3): 637–9. doi:10.1042/bj1170637. PMC 1178970. PMID 5419754.