Uridine-diphosphate-glucose 4-epimerase from Saccharomyces fragilis. Inactivation by heat and reconstitution of the inactive enzyme.
UDP-glucose 4-epimerase from Saccharomyces fragilis is rapidly inactivated by heating at 42 degrees C for 7 min and at 45 degrees C for 4 min. The effector site, specific for sugar phosphates, is destroyed still earlier. The enzyme is inactivated by the dissocation of NAD from it leaving the dimeric structure unaffected. It can be reactivated by mercaptoethanol and NAD, both of which are essential for reactivation, and NAD becomes associated with the dimeric protein moiety.
D002238:Carbohydrate Epimerases / Q000378:metabolism*; D004355:Drug Stability; D004789:Enzyme Activation; D006358:Hot Temperature; D007700:Kinetics; D046911:Macromolecular Substances; D009243:NAD; D011485:Protein Binding; D011489:Protein Denaturation; D012440:Saccharomyces / Q000201:enzymology*; D014534:UDPglucose 4-Epimerase / Q000378:metabolism*
D046911:Macromolecular Substances; D009243:NAD; D002238:Carbohydrate Epimerases; D014534:UDPglucose 4-Epimerase