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Literature summary for 3.2.1.33 extracted from

  • Cheng, A.; Zhang, M.; Okubo, M.; Omichi, K.; Saltiel, A.R.
    Distinct mutations in the glycogen debranching enzyme found in Glycogen Storage Disease Type III lead to impairment in diverse cellular functions (2009), Hum. Mol. Genet., 18, 2045-2052.
    View publication on PubMedView publication on EuropePMC

Application

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

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

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
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