Article ID Journal Published Year Pages File Type
8291600 Archives of Biochemistry and Biophysics 2011 9 Pages PDF
Abstract
► The crystal structure of the hyperthermophilic UDP-galactose 4-epimerase (GalE) was determined. ► The hydrophobic inter-subunit interaction is responsible for the enzyme stability. ► The loop responsible for the tight binding of NAD to the enzyme was identified. ► This is the first report on the structure of a GalE in a hyperthermophile.
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Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
Preview
Crystal structure of UDP-galactose 4-epimerase from the hyperthermophilic archaeon Pyrobaculum calidifontis
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