Abstract
UDPglucose 4-epimerase (EC 5.1.3.2) from Saccharomyces fragilis is a holoenzyme containing 1 mol NAD per mol dimeric protein. The enzyme can be dissociated with p-chloromercuribenzoate and can be reconstituted in the presence of 2-mercaptoethanol and exogenous NAD. Using Cibacron blue F3GA in this reconstituting system, competition between NAD and the dye for the pyridine nucleotide-binding site could be demonstrated. Inactive holoenzyme containing Cibacron blue can also be obtained under these conditions. These data suggest the possible presence of elements of a dinucleotide fold in this enzyme.
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