Observations on the mechanism of the reversible epimerization of GDP-D-mannose to GDP-L-galactose by an enzyme from Chlorella pyrenoidosa

J Biol Chem. 1979 Aug 25;254(16):7600-3.

Abstract

An enzyme fraction from the green alga Chlorella pyrenoidosa that catalyzes the reversible epimerization of guanosine 5'-diphosphate D-mannose to guanosine 5'-diphosphate L-galactose brings about the incorporation of tritium from tritium-labeled water into the hexosyl moieties of those sugar nucleotides. The hexoses were degraded by periodate oxidation whereby the tritium was found to be equally distributed between carbon atoms 3 and 5. That observation was taken to imply that the epimerizations proceed via ene-diol intermediates.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Carbohydrate Epimerases / metabolism*
  • Chlorella / enzymology*
  • Galactose
  • Guanosine Diphosphate Mannose*
  • Guanosine Diphosphate Sugars*
  • Nucleoside Diphosphate Sugars*
  • Oxidation-Reduction
  • Periodic Acid

Substances

  • Guanosine Diphosphate Sugars
  • Nucleoside Diphosphate Sugars
  • Periodic Acid
  • Guanosine Diphosphate Mannose
  • Carbohydrate Epimerases
  • Galactose