PMID:2124547

Citation	Ljungcrantz, P, Bülow, L and Mosbach, K (1990) Construction and characterization of a recombinant tripartite enzyme, galactose dehydrogenase/beta-galactosidase/galactokinase. FEBS Lett. 275:91-4
Abstract	The in-frame gene fusion between 3 enzymes, galactose dehydrogenase, beta-galactosidase and galactokinase, is described. The purified artificial tripartite enzyme displayed all three enzymic activities. Two major forms of the hybrid protein were found, consisting of 4 and 8 subunits respectively, but other forms could also be identified. Each subunit was made up of one monomer each of galactose dehydrogenase, beta-galactosidase and galactokinase. Proximity effects exhibited by the hybrid enzyme could be demonstrated using [14C]galactose as a reporter molecule.
Links	PubMed
Keywords	Base Sequence; Cloning, Molecular/methods; Escherichia coli; Galactokinase/genetics; Galactokinase/metabolism; Galactose/metabolism; Galactose Dehydrogenases/genetics; Galactose Dehydrogenases/metabolism; Genes, Bacterial; Hot Temperature; Hydrogen-Ion Concentration; Molecular Sequence Data; Molecular Weight; Protein Denaturation; Recombinant Fusion Proteins/metabolism; Structure-Activity Relationship; beta-Galactosidase/genetics; beta-Galactosidase/metabolism
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