Biology:UDP-galactopyranose mutase

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UDP-galactopyranose mutase
4u8p.jpg
UDP-galactopyranose mutase tetramer, Aspergillus fumigatus
Identifiers
EC number5.4.99.9
CAS number174632-18-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
UDP-galactopyranose mutase
Identifiers
SymbolUDP-GALP_mutase
InterProIPR004379

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

UDP-D-galactopyranose [math]\displaystyle{ \rightleftharpoons }[/math] 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