UDP-galactopyranose mutase

{{infobox enzyme

| Name = UDP-galactopyranose mutase

| EC_number = 5.4.99.9

| CAS_number = 174632-18-9

| GO_code = 0008767

| image = 4u8p.jpg

| width = 270

| caption = UDP-galactopyranose mutase tetramer, Aspergillus fumigatus

}}

{{Pfam box |Symbol = UDP-GALP_mutase |Name = UDP-galactopyranose mutase |InterPro = IPR004379 |PROSITE = |PDB = {{PDB|1i8t}} }}

In enzymology, an UDP-galactopyranose mutase ({{EnzExplorer|5.4.99.9}}) is an enzyme that catalyzes the chemical reaction

:UDP-D-galactopyranose $\rightleftharpoons$ 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 {{PDB link|1I8T}}, {{PDB link|1V0J}}, {{PDB link|1WAM}}, {{PDB link|2BI7}}, and {{PDB link|2BI8}}.

References

{{cite journal |vauthors=Trejo AG, Chittenden GJ, Buchanan JG, Baddiley J | date = 1970 | title = Uridine diphosphate alpha-D-galactofuranose, an intermediate in the biosynthesis of galactofuranosyl residues | journal = Biochem. J. | volume = 117 | pages = 637–9 | pmid = 5419754 | issue = 3 | doi = 10.1042/bj1170637 | pmc = 1178970 }}

Category:EC 5.4.99

Category:Enzymes of known structure