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Literature summary extracted from

  • Hartley, D.M.; Zhao, C.; Speier, A.C.; Woodard, G.A.; Li, S.; Li, Z.; Walz, T.
    Transglutaminase induces protofibril-like amyloid beta-protein assemblies that are protease-resistant and inhibit long-term potentiation (2008), J. Biol. Chem., 283, 16790-16800.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.3.2.13 medicine TGase can contribute to Alzheimer disease by initiating amyloid beta-protein oligomerization and aggregation at physiological levels, by reducing the clearance of amyloid beta-protein due to the generation of protease-resistant amyloid beta-protein species, and by forming amyloid beta-protein assemblies that inhibit processes involved in memory and learning. TGase might constitute a specific therapeutic target for slowing or blocking the progression of Alzheimer disease Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.13 additional information Homo sapiens TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases ?
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2.3.2.13 additional information Cavia porcellus TGase induces rapid aggregation of amyloid beta-protein within 0.5–30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases ?
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Organism

EC Number Organism UniProt Comment Textmining
2.3.2.13 Cavia porcellus
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2.3.2.13 Homo sapiens
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 recombinantly expressed in Escherichia coli
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.13 liver
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 Cavia porcellus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.13 additional information TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases Homo sapiens ?
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 ?
2.3.2.13 additional information TGase induces rapid aggregation of amyloid beta-protein within 0.5–30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases Cavia porcellus ?
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 ?
2.3.2.13 additional information TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Bothamyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase-induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases Cavia porcellus ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.13 TGase
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 Cavia porcellus
2.3.2.13 TGase
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 Homo sapiens