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UDP-galactopyranose mutase

From Wikipedia, the free encyclopedia
UDP-galactopyranose mutase
UDP-galactopyranose mutase tetramer, Aspergillus fumigatus
Identifiers
EC no.5.4.99.9
CAS no.174632-18-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
UDP-galactopyranose mutase
Identifiers
SymbolUDP-GALP_mutase
InterProIPR004379
Available protein structures:
Pfam   
PDBPDB: 1i8t

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

UDP-D-galactopyranose 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

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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

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  • 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.