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GDP-mannose 3,5-epimerase

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GDP-mannose 3,5-epimerase
Identifiers
EC no.5.1.3.18
CAS no.72162-82-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
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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 GDP-L-galactose + GDP-L-gulose

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.