A transglutaminase is an enzyme that catalyzes the formation of an isopeptide bond between a free amine group (e.g., protein- or peptide-bound lysine) and the acyl group at the end of the side chain of protein- or peptide-bound glutamine. The reaction also produces a molecule of ammonia. Such an enzyme is classified as EC 188.8.131.52. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis).
|PDB structures||RCSB PDB PDBe PDBsum|
Eight transglutaminases have been characterised.
|Factor XIII (fibrin-stabilizing factor)||F13A1, F13B||coagulation||6p25-p24||134570|
|TGM Z||TGM7||testis, lung||15q15.2||606776|
Mechanism of actionEdit
Transglutaminases form extensively cross-linked, generally insoluble protein polymers. These biological polymers are indispensable for an organism to create barriers and stable structures. Examples are blood clots (coagulation factor XIII), as well as skin and hair.
The catalytic reaction is generally viewed as being irreversible, and must be closely monitored through extensive control mechanisms. A collection of the transglutaminase substrate proteins and interaction partners is accessible in the TRANSDAB database.
Role in diseaseEdit
Anti-transglutaminase antibodies are found in celiac disease and may play a role in the small bowel damage in response to dietary gliadin that characterises this condition. In the related condition dermatitis herpetiformis, in which small bowel changes are often found and which responds to dietary exclusion of gliadin-containing wheat products, epidermal transglutaminase is the predominant autoantigen.
Recent research indicates that sufferers from neurological diseases like Huntington's and Parkinson's may have unusually high levels of one type of transglutaminase, tissue transglutaminase. It is hypothesized that tissue transglutaminase may be involved in the formation of the protein aggregates that causes Huntington's disease, although it is most likely not required.
Industrial and culinary applicationsEdit
In commercial food processing, transglutaminase is used to bond proteins together. Examples of foods made using transglutaminase include imitation crabmeat, and fish balls. It is produced by Streptoverticillium mobaraense fermentation in commercial quantities or extracted from animal blood, and is used in a variety of processes, including the production of processed meat and fish products.
Transglutaminase is also used in molecular gastronomy to meld new textures with existing tastes. Besides these mainstream uses, transglutaminase has been used to create some unusual foods. British chef Heston Blumenthal is credited with the introduction of transglutaminase into modern cooking.
- Clarke DD, Mycek MJ, Neidle A, Waelsch H (1959). "The incorporation of amines into proteins". Arch Biochem Biophys. 79: 338–354. doi:10.1016/0003-9861(59)90413-8.
- Pisano JJ, Finlayson JS, Peyton MP (1968). "[Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine.]". Science. 160 (3830): 892–3. Bibcode:1968Sci...160..892P. PMID 4967475. doi:10.1126/science.160.3830.892.
- Griffin M, Casadio R, Bergamini CM (2002). "Transglutaminases: nature's biological glues". Biochem J. 368 (Pt 2): 377–96. PMC . PMID 12366374. doi:10.1042/BJ20021234. Archived from the original on 20 April 2006.
- Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF (1998). "Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes. Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers". J. Biol. Chem. 273 (6): 3452–60. PMID 9452468. doi:10.1074/jbc.273.6.3452.
- Sárdy M, Kárpáti S, Merkl B, Paulsson M, Smyth N (March 2002). "Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis". J. Exp. Med. 195 (6): 747–57. PMC . PMID 11901200. doi:10.1084/jem.20011299.
- Karpuj MV, Becher MW, Steinman L (2002). "Evidence for a role for transglutaminase in Huntington's disease and the potential therapeutic implications". Neurochem. Int. 40 (1): 31–6. PMID 11738470. doi:10.1016/S0197-0186(01)00060-2.
- Vermes I, Steur EN, Jirikowski GF, Haanen C (2004). "Elevated concentration of cerebrospinal fluid tissue transglutaminase in Parkinson's disease indicating apoptosis". Mov. Disord. 19 (10): 1252–4. PMID 15368613. doi:10.1002/mds.20197.
- Lesort M, Chun W, Tucholski J, Johnson GV (2002). "Does tissue transglutaminase play a role in Huntington's disease?". Neurochem. Int. 40 (1): 37–52. PMID 11738471. doi:10.1016/S0197-0186(01)00059-6.
- Köhler, Wim (2008-08-22). "Gelijmde slavink" (in Dutch). NRC Handelsblad. Retrieved 2009-03-05.
- Yokoyama K, Nio N, Kikuchi Y (2004). "Properties and applications of microbial transglutaminase". Appl. Microbiol. Biotechnol. 64 (4): 447–54. PMID 14740191. doi:10.1007/s00253-003-1539-5.
- Jon, Bonné (2005-02-11). "Noodles, reinvented". MSNBC.com. Retrieved 2008-04-02.
- Kelleher, James B. (May 11, 2012). "Industry defends ingredient critics deride as "meat glue"". Chicago Tribune. Retrieved July 20, 2012.
- U.S. Patent 5,156,956 – A transglutaminase catalyzing an acyl transfer reaction of a Γ-carboxyamide group of a glutamine residue in a peptide or protein chain in the absence of Cz2+