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Literature summary for 2.3.2.13 extracted from

  • Siegel, M.; Strnad, P.; Watts, R.E.; Choi, K.; Jabri, B.; Omary, M.B.; Khosla, C.
    Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury (2008), PLoS ONE, 3, e1861.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
(S)-N-(((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-2-(1-(dimethylamino)naphthalene-5-sulfonamido)-3-(1H-indol-3-yl)propanamide the majority of cellular TG2 cannot be inhibited in intact cells. The inhibitor potently inhibits cell lysate TG2 activity in the presence of calcium Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the majority of extracellular TG2 is inactive under normal physiological conditions in cell culture and in vivo. Physical or certain types of chemical injury can lead to rapid enzymatic activation Mus musculus
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Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ calcium in the putrescine incorporation assay buffer results in activation of previously latent TG2 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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Source Tissue

Source Tissue Comment Organism Textmining
small intestine mucosa acute poly(I:C) injury results in rapid TG2 activation Mus musculus
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Synonyms

Synonyms Comment Organism
TG2
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Mus musculus
transglutaminase 2
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Mus musculus