1971Proceedings of the National Academy of SciencesOpen access

Uridine Diphosphate-4-Keto-Glucose, an Intermediate in the Uridine Diphosphate-Galactose-4-Epimerase Reaction

Utpalendu S. Maitra, Helmut Ankel

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Abstract

When UDP-galactose 4-epimerase (EC 5.1.3.2) from Escherichia coli is incubated with UDP-galactose, then reduced with NaB(3)H(4), label is found in UDP-glucose and UDP-galactose. Enzymatic and chemical degradation demonstrates that the label is bound to carbon 4 of the glycosyl moieties. These results provide direct evidence for the existence of UDP-4-keto-glucose as an enzyme-bound intermediate in the epimerization reaction, and they exclude the formation of a 3-keto intermediate.

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When UDP-galactose 4-epimerase (EC 5.1.3.2) from Escherichia coli is incubated with UDP-galactose, then reduced with NaB(3)H(4), label is found in UDP-glucose and UDP-galactose. Enzymatic and chemical degradation demonstrates that the label is bound to carbon 4 of the glycosyl moieties. These results provide direct evidence for the existence of UDP-4-keto-glucose as an enzyme-bound intermediate in the epimerization reaction, and they exclude the formation of a 3-keto intermediate.

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Available abstract

When UDP-galactose 4-epimerase (EC 5.1.3.2) from Escherichia coli is incubated with UDP-galactose, then reduced with NaB(3)H(4), label is found in UDP-glucose and UDP-galactose. Enzymatic and chemical degradation demonstrates that the label is bound to carbon 4 of the glycosyl moieties. These results provide direct evidence for the existence of UDP-4-keto-glucose as an enzyme-bound intermediate in the epimerization reaction, and they exclude the formation of a 3-keto intermediate.

Key concepts: Uridine diphosphate, Uridine diphosphate glucose, Galactose, Nucleotide salvage, Chemistry, Enzyme, Epimer, Uridine

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