Evolutionary-biological peculiarities of transglutaminase. Structure, physiological functions, application

Shleikin, A.; Данилов, Н. П.

doi:10.1134/s0022093011010014

Cited by 20 publications

(22 citation statements)

References 44 publications

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“…Also, well bound are soybean globulins, egg proteins, gliadin, and wheat glutenin Shleikin and Danilov 2011). Thus, MTG-induced gelation, performed under mild conditions, may be a better alternative to encapsulate probiotic cells.…”

Section: Microbial Transglutaminasementioning

confidence: 99%

“…have an anti-inflammatory effect (Da Cruz et al 2013). Recently, new data was published about the importance of TGases in chronic inflammatory diseases, in wound healing, in repair of tissues and development of fibrosis and autoimmune reactions, in chronic degenerative diseases (arthritis, atherosclerosis, and neurodegenerative states), and in oncologic pathology (Shleikin and Danilov 2011). In addition, it is known that TGase causes modification of surface viral glycoproteins gp41 and gp120 that mediate penetration of HIV into cell (Shleikin and Danilov 2011;Tabolacci et al 2012).…”

Section: Microbial Transglutaminasementioning

confidence: 99%

“…Factor XIII helps to stop bleeding by forming cross-links of fibrin molecules and stabilizing fibrin polymers (Faria 2010;Kuraishi et al 2001). In addition, this enzyme is involved in the prevention of blood loss from traumatized vessels by formation of fibrin clot at blood coagulation, activation of platelets, and layering of granulation tissues representing primary healing of local lesion (Shleikin and Danilov 2011). Besides, factor XIII has been applied in the substitutive therapy at rare genetic defects of blood coagulation caused by the absence of TGase in blood plasma (Shleikin and Danilov 2011).…”

Section: Pharmacological Application Of Tgasementioning

confidence: 99%

“…Due to their effects on the physical and chemical properties of proteins, they have many biotechnological applications particularly in the food processing industry, in medicine, and in cosmetics, increasing the demand for an inexpensive, efficient, and safe source of recombinant enzymes (Capell et al 2004;Faria 2010;Serafini-Fracassini and Del Duca 2008;Shleikin and Danilov 2011).…”

Section: Microbial Transglutaminasementioning

confidence: 99%

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Transglutaminases: recent achievements and new sources

Martins

Matos

Costa

et al. 2014

Appl Microbiol Biotechnol

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Transglutaminases are a family of enzymes (EC 2.3.2.13), widely distributed in various organs, tissues, and body fluids, that catalyze the formation of a covalent bond between a free amine group and the γ-carboxamide group of protein or peptide-bound glutamine. Besides forming these bonds, that exhibit high resistance to proteolytic degradation, transglutaminases also form extensively cross-linked, generally insoluble, protein biopolymers that are indispensable for the organism to create barriers and stable structures. The extremely high cost of transglutaminase of animal origin has hampered its wider application and has initiated efforts to find an enzyme of microbial origin. Since the early 1990s, many microbial transglutaminase-producing strains have been found, and production processes have been optimized. This has resulted in a rapidly increasing number of applications of transglutaminase in the food sector. However, applications of microbial transglutaminase in other sectors have also been explored, but in a much lesser extent. Our group has identified a transglutaminase in the oomycete Phytophthora cinnamomi, which is able to induct defense responses and disease-like symptoms. In this mini-review, we report the achievements in this area in order to illustrate the importance and the versatility of transglutaminases.

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Section: Microbial Transglutaminasementioning

confidence: 99%

Section: Microbial Transglutaminasementioning

confidence: 99%

Section: Pharmacological Application Of Tgasementioning

confidence: 99%

Section: Microbial Transglutaminasementioning

confidence: 99%

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Transglutaminases: recent achievements and new sources

Martins

Matos

Costa

et al. 2014

Appl Microbiol Biotechnol

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“…For instance, glycoprotein gp42 present in the cell wall of Phytophthora sojae can induce plenty of defense mechanisms, eliciting a hypersensitive response, resulting in death of the infected cells (21,45). Moreover, some bacterial toxins, including the cytotoxic factor 1 of E. coli, act as a TGase (46). Thus, we propose that SsTGase is secreted from the cytoplasmic membrane and activated by disruptions of the physiological homoeostatic environment after invasion, and then the mature SsTGase could modify the surface proteins of Ss2 and/or host to avoid phagocytosis.…”

Section: Discussionmentioning

confidence: 99%

Functional and Structural Characterization of the Antiphagocytic Properties of a Novel Transglutaminase from Streptococcus suis

Pian

et al. 2015

Journal of Biological Chemistry

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Background: SsTGase was a newly identified secreted immunogenic protein of S. suis 2. Results: Anti-phagocytic ability of SsTGase-N was dependent on its TGase activity, and its crystal structure revealed that dimerization was crucial for maintaining functional activities. Conclusion: SsTGase was a novel virulence factor of Ss2 by acting as a TGase in dimer form. Significance: The presented research suggested that SsTGase could serve as a new therapeutic target.

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The LQSP tetrapeptide is a new highly efficient substrate of microbial transglutaminase for the site‐specific derivatization of peptides and proteins

Caporale

Selis²,

Sandomenico

et al. 2014

Biotechnology Journal

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Transglutaminases catalyze transglutamination reactions on glutamines. Transglutaminases are largely exploited for modifying proteins in pharmaceutical, food, and other biotechnological applications. A library of synthetic peptides has been designed, prepared, and screened to identify new peptide substrates. The new substrates are then used in TGAse-mediated conjugation reactions to engraft synthons onto biomolecules. These peptide substrates confer the bioactive peptides and proteins with new properties. We have identified an optimized substrate named LQSP, which is recognized and processed by microbial TGAse with a strikingly higher efficiency compared to the well-known TQGA sequence. The new substrate has been used to selectively modify prototypical bioactive peptides and proteins with fluoresceine or recognition motifs. We show that, where a reactive lysine is available, proteins and peptides of relevant therapeutic interest, can be selectively and smoothly modified in order to incorporate new functions such as fluorescent labels, recognition units, or reactive groups.

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Evolutionary-biological peculiarities of transglutaminase. Structure, physiological functions, application

Cited by 20 publications

References 44 publications

Transglutaminases: recent achievements and new sources

Transglutaminases: recent achievements and new sources

Functional and Structural Characterization of the Antiphagocytic Properties of a Novel Transglutaminase from Streptococcus suis

The LQSP tetrapeptide is a new highly efficient substrate of microbial transglutaminase for the site‐specific derivatization of peptides and proteins

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