Abstract
UDP-galactose 4-epimerase (EC 5.1.3.2, Gal E) from Escherichia coli catalyzes the reversible reaction between UDP-galactose and UDP-glucose. In this study, the Gal E gene from E. coli, coding UDP-galactose 4-epimerase, was cloned into pYD1 plasmid and then transformed into Saccharomyces cerevisiae EBY100 for expression of Gal E on the cell surface. Enzyme activity analyses with EBY100 cells showed that the enzyme displayed on the yeast cell surface was very active in the conversion between UDP-Glc and UDP-Gal. It took about 3 min to reach equilibrium from UDP-galactose to UDP-glucose.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cloning, Molecular
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DNA, Bacterial / chemistry
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DNA, Bacterial / genetics
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Electrophoresis, Capillary
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Enzymes, Immobilized / genetics
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Enzymes, Immobilized / metabolism*
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Polymerase Chain Reaction
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / genetics
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UDPglucose 4-Epimerase / genetics
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UDPglucose 4-Epimerase / metabolism*
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Uridine Diphosphate Galactose / metabolism
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Uridine Diphosphate Glucose / metabolism
Substances
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DNA, Bacterial
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Enzymes, Immobilized
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Uridine Diphosphate Galactose
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UDPglucose 4-Epimerase
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Uridine Diphosphate Glucose