Application | Comment | Organism |
---|---|---|
medicine | study on patients with Glycogen Storage Disease Type III. Inactivation of either enzymatic activity is sufficient to cause Glycogen Storage Disease Type III disease. The carbohydrate binding domain of amylo-1,6-glucosidase,4-alpha-glucanotransferase plays a major role to coordinate its functions and regulation by the ubiquitin-proteasome system | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
G1448R | mutation detected in patient with Glycogen Storage Disease Type III. Significant loss in both enzymatic activites and carbohydrate binding ability, as well as enhancing targeting for proteasomal degradation | Homo sapiens |
L620P | mutation detected in patient with Glycogen Storage Disease Type III. Mutation abolishes transferase activity | Homo sapiens |
R1147G | mutation detected in patient with Glycogen Storage Disease Type III. Mutation impairs glucosidase function | Homo sapiens |
Y1445ins | mutation detected in patient with Glycogen Storage Disease Type III. Significant loss in both enzymatic activites and carbohydrate binding ability, as well as enhancing targeting for proteasomal degradation | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P35573 | patients with Glycogen Storage Disease Type III. Bifunctional amylo-1,6-glucosidase and 4-alpha-glucanotransferase, protein possesses two separate domains for the transferase and glucosidase activities | - |