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Literature summary extracted from

  • Seigle, J.L.; Celotto, A.M.; Palladino, M.J.
    Degradation of functional triose phosphate isomerase protein underlies sugarkill pathology (2008), Genetics, 179, 855-862.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
5.3.1.1 medicine analysis of key aspects of triosephosphate isomerase deficiency glycolytic enzymopathy pathogenesis identified using the TPIsugarkill mutation M80T, a Drosophila model of the human disease deficiency. Mutant protein is expressed, capable of forming a homodimer, and is functional. However, the mutant protein is degraded by the 20S proteasome core leading to loss-of-function pathogenesis Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.1 M80T analysis of key aspects of triosephosphate isomerase deficiency glycolytic enzymopathy pathogenesis identified using the TPIsugarkill mutation M80T, a Drosophila model of the human disease deficiency. Mutant protein is expressed, capable of forming a homodimer, and is functional. However, the mutant protein is degraded by the 20S proteasome core leading to loss-of-function pathogenesis Drosophila melanogaster

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.1 26500
-
 2 * 26500, SDS-PAGE, both wild-type and mutant M80T Drosophila melanogaster
5.3.1.1 53000
-
 gel filtration, both wild-type and mutant M80T Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.1 Drosophila melanogaster
-
-
-

Subunits

EC Number Subunits Comment Organism
5.3.1.1 dimer 2 * 26500, SDS-PAGE, both wild-type and mutant M80T Drosophila melanogaster