Transglutaminase

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Transglutaminases are a family of enzymes (EC 2.3.2.13) that catalyze the formation of a covalent bond between a free amine group (e.g., protein- or peptide-bound lysine) and the gamma-carboxamid group of protein- or peptide-bound glutamine. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation.

Transglutaminases were first described in 1959.[1]. The exact biochemical activity of transglutaminases was discovered in blood coagulation protein factor XIII in 1968.[2]

Physiological transglutaminases

Eight transglutaminases have been characterised.[3]

Name Gene Activity Chromosome OMIM
Factor XIII (fibrin-stabilizing factor) F13A1, F13B coagulaton 6p25-p24 134570
Keratinocyte transglutaminase TGM1 skin 14q11.2 190195
Tissue transglutaminase TGM2 ubiquitous 20q11.2-q12 190196
Epidermal transglutaminase TGM3 skin 20q12 600238
Prostate transglutaminase TGM4 prostate 3p22-p21.33 600585
TGM X TGM5[4] skin 15q15.2 603805
TGM Y TGM6 unclear 20q11-15 not assigned
TGM Z TGM7 testis, lung 15q15.2 606776

Mechanism of action

Transglutaminases form extensively cross-linked, generally insoluble protein polymers. These biological polymers are indispensable for the organism in order 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.[3] A collection of the transglutaminase substrate proteins and interaction partners is accessible in the TRANSDAB database.

Role in disease

Deficiency of factor XIII (a rare genetic condition) predisposes to hemorrhage; concentrated enzyme can be used to correct the abnormality and reduce bleeding risk.[3]

Antibodies to tissue transglutaminase are found in coeliac disease and may play a role in the small bowel damage in response to dietary gliadin that characterises this condition.[3]

Recent research indicates that sufferers from neurological diseases like Huntington's,[5] and Parkinson's[6] 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.[7][3]

Industrial applications

Industrial transglutaminase is produced by Streptomyces mobaraensis fermentation in commercial quantities and is used in a variety of processes, including the production of processed meat and fish products. It can be used as a binding agent to improve the texture of protein-rich foods such as surimi or ham.[8]

Transglutaminase can be used in these applications:[citation needed]

  • Binding small chunks of meats into a big one ("portion control"), such as in sausages, hot dogs, restructured steaks
  • Improving the texture of low-grade meat such as so-called "PSE meat" (pale, soft, and exudative meat, whose characteristics are attributed to stress and a rapid postmortem pH decline)
  • Making milk and yogurt creamier
  • Making noodles firmer

Besides these mainstream uses, transglutaminase has been used to create some unusual foods. British chef Heston Blumenthal is credited with the introduction of "meat glue" into modern cooking. Wylie Dufresne, chef of New York's avant-garde restaurant wd~50, was introduced to transglutaminase by Blumenthal, and invented a "pasta" made by over 95% shrimps thanks to transglutaminase.[9]

See also

References

  1. 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.
  2. Pisano JJ, Finlayson JS, Peyton MP (1968). "[Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine.]". Science. 160 (830): 892–3. doi:10.1126/science.160.3830.892. PMID 4967475.
  3. 3.0 3.1 3.2 3.3 3.4 Griffin M, Casadio R, Bergamini CM (2002). "Transglutaminases: nature's biological glues". Biochem J. 368(Pt 2): 377–96. doi:10.1042/BJ20021234. PMID 12366374. PMC 1223021
  4. 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. doi:10.1074/jbc.273.6.3452. PMID 9452468.
  5. 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. doi:10.1016/S0197-0186(01)00060-2. PMID 11738470.
  6. 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. doi:10.1002/mds.20197. PMID 15368613.
  7. 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. doi:10.1016/S0197-0186(01)00059-6. PMID 11738471.
  8. Yokoyama K, Nio N, Kikuchi Y (2004). "Properties and applications of microbial transglutaminase". Appl. Microbiol. Biotechnol. 64 (4): 447–54. doi:10.1007/s00253-003-1539-5. PMID 14740191.
  9. Jon, Bonné (2005-02-11). "Noodles, reinvented". MSNBC.com. Retrieved 2008-04-02.

External links

de:Transglutaminase it:Transglutaminasi fi:Glutamyylitransferaasi


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