UDP-galactopyranose mutase
| UDP-galactopyranose mutase | |||||||||
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UDP-galactopyranose mutase tetramer, Aspergillus fumigatus
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| Identifiers | |||||||||
| EC number | 5.4.99.9 | ||||||||
| CAS number | 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 / EGO | ||||||||
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| Search | |
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| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
| UDP-galactopyranose mutase | |
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| Identifiers | |
| Symbol | UDP-GALP_mutase |
| InterPro | IPR004379 |
In enzymology, an UDP-galactopyranose mutase (EC 5.4.99.9) is an enzyme that catalyzes the chemical reaction
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.
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.
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