UDP-galactopyranose mutase
UDP-galactopyranose mutase | |||||||||
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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 | ||||||||
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UDP-galactopyranose mutase | |||||||
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Identifiers | |||||||
Symbol | UDP-GALP_mutase | ||||||
InterPro | IPR004379 | ||||||
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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
[edit]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
[edit]- 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.