GDP-mannose 3,5-epimerase
In enzymology, a GDP-mannose 3,5-epimerase (EC 5.1.3.18) is an enzyme that catalyzes the chemical reaction
- GDP-mannose GDP-L-galactose + GDP-L-gulose
| GDP-mannose 3,5-epimerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 5.1.3.18 | ||||||||
| CAS number | 72162-82-4 | ||||||||
| 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 | ||||||||
| |||||||||
Hence, this enzyme has one substrate, GDP-mannose, and two products, GDP-L-galactose and GDP-L-gulose
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is GDP-mannose 3,5-epimerase. Other names in common use include GDP-D-mannose:GDP-L-galactose epimerase, guanosine 5'-diphosphate D-mannose:guanosine 5'-diphosphate, and L-galactose epimerase. This enzyme participates in ascorbate and aldarate metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 2C54, 2C59, 2C5A, and 2C5E.
References
- Barber GA, Hebda PA (1982). "GDP-D-mannose: GDP-L-galactose epimerase from Chlorella pyrenoidosa". Methods Enzymol. Methods in Enzymology. 83: 522–5. doi:10.1016/0076-6879(82)83046-2. ISBN 978-0-12-181983-5. PMID 7098948.
- Hebda PA, Behrman EJ, Barber GA (1979). "The guanosine 5'-diphosphate D-mannose: guanosine 5'-diphosphate L-galactose epimerase of Chlorella pyrenoidosa. Chemical synthesis of guanosine 5'-diphosphate L-galactose and further studies of the enzyme and the reaction it catalyzes". Arch. Biochem. Biophys. 194 (2): 496–502. doi:10.1016/0003-9861(79)90644-1. PMID 443816.
- Gevaert O, Van Overtveldt S, Beerens K, Desmet T (2019). "Characterization of the First Bacterial and Thermostable GDP-Mannose 3,5-Epimerase". Int. J. Mol. Sci. 20 (14): E3530. doi:10.3390/ijms20143530. PMID 31330931.