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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Immobilization of UDP-Galactose 4-Epimerase from Escherichia coli on the Yeast Cell Surface.

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.[1]

References

  1. Immobilization of UDP-Galactose 4-Epimerase from Escherichia coli on the Yeast Cell Surface. Zhang, H.C., Bi, J.Y., Chen, C., Huang, G.L., Qi, Q.S., Xiao, M., Wang, P.G. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
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