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Literature summary for 5.3.1.1 extracted from

  • Park, S.A.; Park, H.W.; Kim, N.H.; Kim, Y.H.; Kwak, M.J.; Shin, J.S.; Kim, C.W.
    Effects of Tau on the activity of triose phosphate isomerase (TPI) in brain cells (2010), Neurochem. Int., 56, 886-892.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information some TPIs are found on the paired helical filaments in Tau transgenic mice Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
additional information recombinant expression of Tau in CHO-K1 cells leads to increased protection of TPI against oxidative damage, but also to decreased enzyme activity, with unaltered TPI expression levels Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-Glyceraldehyde 3-phosphate Mus musculus
-
Glycerone phosphate
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glyceraldehyde 3-phosphate
-
Mus musculus Glycerone phosphate
-
?
additional information Tau, main component of the aberrant paired helical filaments found in Alzheimer's disease, interacts with the enzyme and protects TPI against oxidative damage, overview. Interaction between Tau and triose phosphate isomerase occurs in a normal, nondisease state as well as in a neurodegeneration state Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
TpI
-
Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mus musculus