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Literature summary for 2.3.2.13 extracted from

  • Pina Dore, M.; Pes, G.M.; Errigo, A.; Manca, A.; Realdi, G.
    Tissue transglutaminase activity in human gastric mucosa according to Helicobacter pylori infection (2018), Exp. Biol. Med. (Maywood), 243, 1161-1164 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information in normal conditions, t-TG in the cytosol and extracellular matrix is predominantly in a closed conformation, maintained by guanine nucleotide and/or integrin bindings. Physical or chemical injury opens the conformation and activates the enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-
extracellular extracellular matrix Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the enzyme is calcium-dependent Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein glutamine + alkylamine Homo sapiens
-
protein N5-alkylglutamine + NH3
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P21980
-
-

Source Tissue

Source Tissue Comment Organism Textmining
gastric mucosa patients with Helicobacter pylori negative gastritis have higher t-TG activity than patients with healthy, unifected gastric mucosa Homo sapiens
-
stomach
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethyl casein glutamine + putrescine
-
Homo sapiens ?
-
?
protein glutamine + alkylamine
-
Homo sapiens protein N5-alkylglutamine + NH3
-
?

Synonyms

Synonyms Comment Organism
t-TG
-
Homo sapiens
tissue transglutaminase
-
Homo sapiens
tissue-TG
-
Homo sapiens

Expression

Organism Comment Expression
Homo sapiens antral t-TG activity is significantly increased in Helicobacter pylori positive patients compared to Helicobacter pylori negative patients. The activity of t-TG is higher in patients harboring cagA positive strains vs. cagA negative strains up

General Information

General Information Comment Organism
physiological function tissue transglutaminase (t-TG) is a multifunctional protein involved in the healing of gastric erosions and ulcers in animal models. Determination of increased gastric t-TG activity in patients with dyspepsia according to Helicobacter pylori infection and cytotoxin-associated gene A (cagA) and vacuolating cytotoxin (vacA) subtype status. t-TG activity is significantly greater in gastritis associated with Helicobacter pylori infection, suggesting that this enzyme is induced by inflammation and may have an important role in the natural history of human gastritis. Tissue-TG is expressed at sites of inflammation, and can act as a modulator of inflammation, exerting both pro- and anti-inflammatory effects. The enzyme covalently cross-links a variety of proteins in the extracellular matrix, increasing fibrosis in order to favor wound healing by increasing resistance to chemical, enzymatic, and physical disruption Homo sapiens