PMID:9224707

Citation	Nayar, S and Bhattacharyya, D (1997) UDP-galactose 4-epimerase from Escherichia coli: existence of a catalytic monomer. FEBS Lett. 409:449-51
Abstract	UDP-galactose 4-epimerase from Escherichia coli is a homodimer of molecular mass 39 kDa/subunit and requires NAD as a co-factor. X-ray crystallographic studies indicate two pyridine nucleotide co-factor-binding sites of the dimeric molecule situated in a symmetry-oriented manner. Size-exclusion HPLC of an equilibrium intermediate at 3 M urea suggests a monomeric holoenzyme structure that is catalytically active. Ultracentrifugal studies of the native enzyme in a 5-20% sucrose gradient at low protein concentration also indicate existence of a catalytic monomer. The monomer resembles the dimeric protein in stability and most of its physico-chemical properties.
Links	PubMed
Keywords	Anilino Naphthalenesulfonates; Binding Sites; Catalysis; Chromatography, High Pressure Liquid; Crystallography, X-Ray; Enzyme Activation; Escherichia coli/chemistry; Escherichia coli/enzymology; Fluorescent Dyes; Osmolar Concentration; Protein Denaturation; UDPglucose 4-Epimerase/chemistry; UDPglucose 4-Epimerase/isolation & purification; UDPglucose 4-Epimerase/metabolism
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