Transglutaminase

From Wikipedia, the free encyclopedia

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 1957.^[1]. The exact biochemical activity of transglutaminases was discovered in blood coagulation protein factor XIII in 1968.^[2]

Contents 1 Physiological transglutaminases 2 Mechanism of action 3 Role in disease 4 Industrial applications 5 See also 6 References 7 External links

[edit] Physiological transglutaminases

Eight transglutaminases have been characterised.^[3]

Name	Activity	Chromosome	OMIM
Factor XIII (fibrin-stabilizing factor)	coagulaton	6p25-p24	Mendelian Inheritance in Man (OMIM) 134570
Keratinocyte transglutaminase (TGM1)	skin	14q11.2	Mendelian Inheritance in Man (OMIM) 190195
Tissue transglutaminase (TGM2)	ubiquitous	20q11.2-q12	Mendelian Inheritance in Man (OMIM) 190196
Epidermal transglutaminase (TGM3)	skin	20q12	Mendelian Inheritance in Man (OMIM) 600238
Prostate transglutaminase (TGM4)	prostate	3p22-p21.33	Mendelian Inheritance in Man (OMIM) 600585
TGM X or TGM5[4]	skin	15q15.2	Mendelian Inheritance in Man (OMIM) 603805
TGM Y or TGM 6	unclear	20q11-15	not assigned
TGM Z or TGM 7	testis, lung	15q15.2	Mendelian Inheritance in Man (OMIM) 606776

[edit] 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.

[edit] 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.

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.

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]

[edit] 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.

Transglutaminase can be used in these applications:

• 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; caused by stress and a rapid postmortem pH decline)
• Making milk and yogurt creamier
• Making noodles firmer

Besides its "orthodox" uses, transglutaminase can be used to create some unusual foods. "Cold Set Bound Fish Kebabs" are made from alternating layers of salmon and cod which are "glued" together by transglutaminase. Wylie Dufresne, chef of New York's avant-garde restaurant WD-50, invented a "pasta" made by over 95% shrimps thanks to transglutaminase.

[edit] See also

• Surimi
• Boneless Fish

[edit] References

1. ^ Clarke DD, Mycek MJ, Neidle A, Waelsch H. The incorporation of amines into proteins. Arch Biochem Biophys 1957;79:338–354.
2. ^ Pisano JJ, Finlayson JS, Peyton MP. Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine. Science 1968;160:892-3. PMID 4967475.
3. ^ Griffin M, Casadio R, Bergamini CM. Transglutaminases: nature's biological glues. Biochem J 2002;368(Pt 2):377-96. PMID 12366374.
4. ^ Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF. Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes. J Biol Chem 1998;273:3452-3460. PMID 9452468.
5. ^ Karpuj MV, Becher MW, Steinman L. Evidence for a role for transglutaminase in Huntington's disease and the potential therapeutic implications. Neurochem Int 2002;40:31-6. PMID 11738470.
6. ^ Vermes I, Steur EN, Jirikowski GF, Haanen C. Elevated concentration of cerebrospinal fluid tissue transglutaminase in Parkinson's disease indicating apoptosis. Mov Disord 2004;19(10):1252-4. PMID 15368613.
7. ^ Lesort M, Chun W, Tucholski J, Johnson GV. Does tissue transglutaminase play a role in Huntington's disease? Neurochem Int 2002;40:37-52. PMID 11738471.

[edit] External links

• Enzyme for Binder and Texture improver
• Ajinomoto Co's Transglutaminase Activa
• Noodles, reinvented (MSNBC)