GDP-mannose 3,5-epimerase

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In enzymology, a GDP-mannose 3,5-epimerase (EC 5.1.3.18) is an enzyme that catalyzes the chemical reaction

GDP-mannose $\rightleftharpoons$ GDP-L-galactose

Hence, this enzyme has one substrate, GDP-mannose, and one product, GDP-L-galactose.

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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 5.1.3.18
BRENDA references for 5.1.3.18 (Recommended.)
PubMed references for 5.1.3.18
PubMed Central references for 5.1.3.18
Google Scholar references for 5.1.3.18
Barber GA, Hebda PA (1982). "GDP-D-mannose: GDP-L-galactose epimerase from Chlorella pyrenoidosa". Methods. Enzymol. 83: 522–5. 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: 496–502. PMID 443816.