| 词条 | Transglutaminase | |||||||||||||||||||||||||||||||||||||||||||||
| 释义 |
|name=Transglutaminase| image =Coagulation factor XIII 1EVU.png | caption =Transglutaminase example: coagulation factor XIII from human blood. PDB code: 1EVU. | EC_number = 2.3.2.13 | CAS_number = 80146-85-6 | GO_code = | Name = | IUBMB_EC_number = 2/3/2/13 | width = }}Transglutaminases are enzymes that in nature primarily catalyze the formation of an isopeptide bond between γ-carboxamide groups ( -(C=O)NH2 ) of glutamine residue side chains and the ε-amino groups ( -NH3 ) of lysine residue side chains with subsequent release of ammonia ( NH3 ). Lysine and glutamine residues must be bound to a peptide or a protein so that this cross-linking (between separate molecules) or intermolecular (within the same molecule) reaction can happen.[1] Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis).[2] The reaction is[1] Gln-(C=O)NH2 + NH2-Lys → Gln-(C=O)NH-Lys + NH3 Transglutaminases can also join a primary amine ( RNH2 ) to the side chain carboxyamide group of a protein/peptide bound glutamine residue thus forming an isopeptide bond[1] Gln-(C=O)NH2 + RNH2 → Gln-(C=O)NHR + NH3 These enzymes can also deamidate glutamine residues to glutamic acid residues in the presence of water[1] Gln-(C=O)NH2 + H2O → Gln-COOH + NH3 Transglutaminase isolated from Streptomyces mobaraensis -bacteria for example, is a calcium-independent enzyme. Mammalian transglutaminases among other transglutaminases require Ca2+ ions as a cofactor.[1] Transglutaminases were first described in 1959.[2] The exact biochemical activity of transglutaminases was discovered in blood coagulation protein factor XIII in 1968.[3] Physiological transglutaminasesEight transglutaminases have been characterised.[4]
Biological roleTransglutaminases 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.[4] A collection of the transglutaminase substrate proteins and interaction partners is accessible in the TRANSDAB database. Role in diseaseDeficiency of factor XIII (a rare genetic condition) predisposes to hemorrhage; concentrated enzyme can be used to correct the abnormality and reduce bleeding risk.[4] 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.[4] 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.[6]Recent research indicates that sufferers from neurological diseases like Huntington's[7] and Parkinson's[8] 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.[4][9] Mutations in keratinocyte transglutaminase are implicated in lamellar ichthyosis. Industrial and culinary applicationsIn 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,[10] and is used in a variety of processes, including the production of processed meat and fish products. Transglutaminase can be used as a binding agent to improve the texture of protein-rich foods such as surimi or ham.[11] So-called "Meat glue" made from bovine and porcine sources was banned throughout the European Union as a food additive in 2010.[12] Transglutaminase remains allowed and is not required to be declared, as it is considered a processing aid and not an additive which remains present in the final product. Molecular gastronomyTransglutaminase 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. Wylie Dufresne, chef of New York's avant-garde restaurant wd~50, was introduced to transglutaminase by Blumenthal, and invented a "pasta" made from over 95% shrimp thanks to transglutaminase.[13]See also
References1. ^1 2 3 4 {{Cite journal|last=DeJong|first=GAH|last2=Koppelman|first2=SJ|date=2002|title=Transglutaminase Catalyzed Reactions: Impact on Food Applications|journal=Journal of Food Science|volume=67|issue=8|pages=2798–2806|doi=10.1111/j.1365-2621.2002.tb08819.x|issn=0022-1147}} 2. ^{{Cite journal|vauthors=Clarke DD, Mycek MJ, Neidle A, Waelsch H |title=The incorporation of amines into proteins| journal=Arch Biochem Biophys| year=1959| volume=79| pages=338–354 | doi=10.1016/0003-9861(59)90413-8}} 3. ^{{Cite journal|vauthors=Pisano JJ, Finlayson JS, Peyton MP |title=[Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine.] |journal=Science |volume=160 |issue=3830 |pages=892–3 |year=1968 |pmid=4967475 |doi=10.1126/science.160.3830.892|bibcode=1968Sci...160..892P }} 4. ^1 2 3 4 5 {{Cite journal|vauthors=Griffin M, Casadio R, Bergamini CM |title=Transglutaminases: nature's biological glues |journal=Biochem J |year=2002 |volume=368 |pages=377–96 |pmid=12366374 |doi=10.1042/BJ20021234 |issue=Pt 2 |pmc=1223021 }} 5. ^{{Cite journal |vauthors=Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF |title=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 |journal=J. Biol. Chem. |volume=273 |issue=6 |pages=3452–60 |year=1998 |pmid=9452468 |doi=10.1074/jbc.273.6.3452 |df=dmy-all }} 6. ^{{Cite journal |vauthors=Sárdy M, Kárpáti S, Merkl B, Paulsson M, Smyth N |title=Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis |journal=J. Exp. Med. |volume=195 |issue=6 |pages=747–57 |date=March 2002 |pmid=11901200 |pmc=2193738 |doi=10.1084/jem.20011299 |df=dmy-all }} 7. ^{{Cite journal|vauthors=Karpuj MV, Becher MW, Steinman L |title=Evidence for a role for transglutaminase in Huntington's disease and the potential therapeutic implications |journal=Neurochem. Int. |volume=40 |issue=1 |pages=31–6 |year=2002 |pmid=11738470 |doi=10.1016/S0197-0186(01)00060-2}} 8. ^{{Cite journal|vauthors=Vermes I, Steur EN, Jirikowski GF, Haanen C |title=Elevated concentration of cerebrospinal fluid tissue transglutaminase in Parkinson's disease indicating apoptosis |journal=Mov. Disord. |volume=19 |issue=10 |pages=1252–4 |year=2004 |pmid=15368613 |doi=10.1002/mds.20197}} 9. ^{{Cite journal|vauthors=Lesort M, Chun W, Tucholski J, Johnson GV |title=Does tissue transglutaminase play a role in Huntington's disease? |journal=Neurochem. Int. |volume=40 |issue=1 |pages=37–52 |year=2002 |pmid=11738471 |doi=10.1016/S0197-0186(01)00059-6}} 10. ^{{Cite news |last = Köhler |first = Wim |title = Gelijmde slavink |work = |pages = |language = Dutch |publisher = NRC Handelsblad |date = 2008-08-22 |url = http://www.nrc.nl/achtergrond/article1960242.ece/Gelijmde_slavink |accessdate = 2009-03-05 |deadurl = no |archiveurl = https://web.archive.org/web/20090220132207/http://www.nrc.nl/achtergrond/article1960242.ece/Gelijmde_slavink |archivedate = 20 February 2009 |df = dmy-all}} 11. ^{{Cite journal|vauthors=Yokoyama K, Nio N, Kikuchi Y |title=Properties and applications of microbial transglutaminase |journal=Appl. Microbiol. Biotechnol. |volume=64 |issue=4 |pages=447–54 |year=2004 |pmid=14740191 |doi=10.1007/s00253-003-1539-5}} 12. ^{{cite web|url=http://www.foodsafetynews.com/2010/05/eu-bans-meat-glue/#.WsTo0TDTVyU|title=EU Bans 'Meat Glue' - Food Safety News|author=|date=24 May 2010|website=foodsafetynews.com|accessdate=6 May 2018|deadurl=no|archiveurl=https://web.archive.org/web/20180405025014/http://www.foodsafetynews.com/2010/05/eu-bans-meat-glue/#.WsTo0TDTVyU|archivedate=5 April 2018|df=dmy-all}} 13. ^{{Cite news |first=Bonné |last=Jon |title=Noodles, reinvented |url=http://www.msnbc.msn.com/id/6915287/ |work=MSNBC.com |date=2005-02-11 |accessdate=2008-04-02 |deadurl=no |archiveurl=https://web.archive.org/web/20080312035146/http://www.msnbc.msn.com/id/6915287/ |archivedate=12 March 2008 |df=dmy-all }} Additional sources
3 : EC 2.3.2|Food additives|Autoantigens |
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