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

作者：George A. Barber · 发表于：Journal of Biological Chemistry · 年份：1979 · DOI：10.1016/s0021-9258(18)35986-6 · 被引用次数：41 · 研究领域：Amino Acid Enzymes and Metabolism、Polyamine Metabolism and Applications、Enzyme Structure and Function

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.