The presence of elements of a dinucleotide fold in UDP-glucose 4-epimerase from Saccharomyces fragilis.
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.
D000873:Anthracenes; D002238:Carbohydrate Epimerases / Q000378:metabolism*; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004396:Coloring Agents; D007700:Kinetics; D008623:Mercaptoethanol / Q000494:pharmacology; D009243:NAD / Q000032:analysis*; D011485:Protein Binding; D011487:Protein Conformation; D012440:Saccharomyces / Q000201:enzymology*; D014227:Triazines; D014534:UDPglucose 4-Epimerase / Q000378:metabolism*; D020245:p-Chloromercuribenzoic Acid
D000873:Anthracenes; D002729:Chloromercuribenzoates; D004396:Coloring Agents; D014227:Triazines; D009243:NAD; D020245:p-Chloromercuribenzoic Acid; C012842:Cibacron Blue F 3GA; D008623:Mercaptoethanol; D002238:Carbohydrate Epimerases; D014534:UDPglucose 4-Epimerase