Biology:Glucuronate isomerase
| glucuronate isomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 5.3.1.12 | ||||||||
| CAS number | 9023-87-4 | ||||||||
| 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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In enzymology, a glucuronate isomerase (EC 5.3.1.12) is an enzyme that catalyzes the chemical reaction
- D-glucuronate [math]\displaystyle{ \rightleftharpoons }[/math] D-fructuronate
Hence, this enzyme has one substrate, D-glucuronate, and one product, D-fructuronate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D-glucuronate aldose-ketose-isomerase. Other names in common use include uronic isomerase, uronate isomerase, D-glucuronate isomerase, uronic acid isomerase, and D-glucuronate ketol-isomerase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1J5S and 2Q01.
References
- "Uronic acid metabolism in bacteria. I. Purification and properties of uronic acid isomerase in Escherichia coli". J. Biol. Chem. 235: 1559–1565. 1960. PMID 13794771.
- "Catabolism of galacturonic and glucuronic acids by Erwinia carotovora". J. Biol. Chem. 234: 2227–35. 1959. PMID 14409051.
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