Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2048018 | FEBS Letters | 2012 | 4 Pages |
The X-ray structure of rabbit glycogenin containing the T82M (T83M according to previous authors amino acid numbering [1]) mutation causing glycogenosis showed the loss of Thr82 hydrogen bond to Asp162, the residue involved in the activation step of the glucose transfer reaction mechanism. Autoglucosylation, maltoside transglucosylation and UDP-glucose hydrolyzing activities were abolished even though affinity and interactions with UDP-glucose and positioning of Tyr194 acceptor were conserved. Substitution of Thr82 for serine but not for valine restored the maximum extent of autoglucosylation as well as transglucosylation and UDP-glucose hydrolysis rate. Results provided evidence sustaining the essential role of the lost single hydrogen bond for UDP-glucose activation leading to glycogenin-bound glycogen primer synthesis.
► T82M mutation does not change contacts with UDPG and Tyr194 positioning. ► Autoglucosylation, DBM glucosylation and UDPG hydrolysis are abolished in T82M mutant. ► Glucose transfer activities are lost by Val but not by Ser substitution of Thr82.