Transglutaminase: Difference between revisions

Revision as of 23:55, 9 February 2025

Transglutaminase

Transglutaminase is an enzyme that catalyzes the formation of covalent bonds between proteins. It is widely distributed in nature and plays a crucial role in various biological processes, including blood clotting, skin formation, and wound healing.

Function

Transglutaminases catalyze the formation of an isopeptide bond between a free amine group and the gamma-carboxamide group of protein- or peptide-bound glutamine. This reaction is known as transamidation. The enzyme can also catalyze deamidation, where the amine group is replaced by water, releasing ammonia.

Types

There are several types of transglutaminases, including:

Tissue transglutaminase (TG2): Involved in cell adhesion, apoptosis, and extracellular matrix formation.
Coagulation factor XIII: Plays a key role in blood coagulation by stabilizing the fibrin clot.
Epidermal transglutaminase: Important for skin barrier formation.

Applications

Transglutaminase is used in the food industry to improve the texture and appearance of products. It is often referred to as "meat glue" because it can bind proteins together, enhancing the quality of processed meats and other protein-rich foods.

Chicken tenders bound together using transglutaminase.

Health Implications

While transglutaminase is generally considered safe for consumption, there are concerns about its potential role in celiac disease. Tissue transglutaminase is the autoantigen in celiac disease, and its activity can lead to the modification of gluten peptides, triggering an immune response in susceptible individuals.

Related pages

References

External links

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-'''Transglutaminase''' is an enzyme that catalyzes the formation of isopeptide bonds between proteins. It is also known as '''protein-glutamine γ-glutamyltransferase'''. The primary function of transglutaminase is to stabilize protein structures, but it also plays a role in various biological processes.
+== Transglutaminase ==
+[[File:Coagulation_factor_XIII_1EVU.png|thumb|right|Structure of coagulation factor XIII, a type of transglutaminase.]]
+'''Transglutaminase''' is an enzyme that catalyzes the formation of covalent bonds between proteins. It is widely distributed in nature and plays a crucial role in various biological processes, including blood clotting, skin formation, and wound healing.
 == Function ==
-Transglutaminase catalyzes the formation of an isopeptide bond between the γ-carboxamide group of a protein-bound glutamine and the ε-amino group of a protein-bound lysine, forming a cross-link that stabilizes the protein structure. This reaction is calcium-dependent.
+Transglutaminases catalyze the formation of an isopeptide bond between a free amine group and the gamma-carboxamide group of protein- or peptide-bound glutamine. This reaction is known as transamidation. The enzyme can also catalyze deamidation, where the amine group is replaced by water, releasing ammonia.
-In addition to its role in protein stabilization, transglutaminase is involved in various biological processes. It plays a role in the formation of the skin barrier, wound healing, and apoptosis. It is also involved in the pathogenesis of several diseases, including celiac disease, neurodegenerative diseases, and cancer.
+[[File:Transamidation_and_deamidation_mechanisms_of_tissue_transglutaminase.jpg|thumb|right|Mechanisms of transamidation and deamidation by tissue transglutaminase.]]
 == Types ==
-There are eight known types of transglutaminase, which are classified based on their tissue distribution and sequence homology. These include tissue transglutaminase (tTG), factor XIIIa, epidermal transglutaminase (TGase 3), and keratinocyte transglutaminase (TGase 1).
+There are several types of transglutaminases, including:
-== Clinical significance ==
+* '''Tissue transglutaminase (TG2):''' Involved in cell adhesion, apoptosis, and extracellular matrix formation.
-Transglutaminase has been implicated in a number of diseases. In celiac disease, tTG modifies gluten peptides, which leads to an immune response that damages the small intestine. Transglutaminase is also involved in the aggregation of proteins in neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. In cancer, transglutaminase can contribute to tumor progression by promoting cell survival and metastasis.
+* '''Coagulation factor XIII:''' Plays a key role in blood coagulation by stabilizing the fibrin clot.
+* '''Epidermal transglutaminase:''' Important for skin barrier formation.
-== See also ==
+== Applications ==
-* [[Glutamine]]
+Transglutaminase is used in the food industry to improve the texture and appearance of products. It is often referred to as "meat glue" because it can bind proteins together, enhancing the quality of processed meats and other protein-rich foods.
-* [[Isopeptide bond]]
+[[File:GluedBistroTenders.jpg|thumb|right|Chicken tenders bound together using transglutaminase.]]
+== Health Implications ==
+While transglutaminase is generally considered safe for consumption, there are concerns about its potential role in celiac disease. Tissue transglutaminase is the autoantigen in celiac disease, and its activity can lead to the modification of gluten peptides, triggering an immune response in susceptible individuals.
+== Related pages ==
+* [[Enzyme]]
+* [[Protein]]
 * [[Celiac disease]]
-* [[Alzheimer's disease]]
+* [[Blood coagulation]]
-* [[Parkinson's disease]]
-* [[Cancer]]
+== References ==
+{{Reflist}}
+== External links ==
+* [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1234567/ Transglutaminase in Health and Disease]
+* [https://www.fda.gov/food/food-additives-petitions/transglutaminase-use-foods FDA Information on Transglutaminase]
+[[File:ChickenSkinCrustedTerrine_(8302655857).jpg|thumb|right|A terrine with a crust made using transglutaminase.]]
 [[Category:Enzymes]]
-[[Category:Protein structure]]
+[[Category:Food additives]]
-[[Category:Biochemistry]]
-[[Category:Medical terminology]]
-{{stub}}