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Literature summary for 5.3.1.1 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
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Application

Application Comment Organism
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

Protein Variants Comment Organism
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]

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

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Subunits

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