Molecular and Catalytic Properties of Transglutaminases

Folk, J.E.; Chung, Soo‐Il

doi:10.1002/9780470122839.ch3

Cited by 115 publications

(33 citation statements)

References 81 publications

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“…Transglutaminases catalyse the acyl transfer between the γ-carboxyamide of a peptide bound glutamine (acyl donor) to a primary amine (acyl acceptor). When water functions as an acyl acceptor the result is glutamine deamidation [38]. The choice between deamidation and transglutamination is influenced by the environment of the targeted glutamine residue [39], [40].…”

Section: Discussionmentioning

confidence: 99%

Modification of Heterotrimeric G-Proteins in Swiss 3T3 Cells Stimulated with Pasteurella multocida Toxin

et al. 2012

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Many bacterial toxins covalently modify components of eukaryotic signalling pathways in a highly specific manner, and can be used as powerful tools to decipher the function of their molecular target(s). The Pasteurella multocida toxin (PMT) mediates its cellular effects through the activation of members of three of the four heterotrimeric G-protein families, Gq, G12 and Gi. PMT has been shown by others to lead to the deamidation of recombinant Gαi at Gln-205 to inhibit its intrinsic GTPase activity. We have investigated modification of native Gα subunits mediated by PMT in Swiss 3T3 cells using 2-D gel electrophoresis and antibody detection. An acidic change in the isoelectric point was observed for the Gα subunit of the Gq and Gi families following PMT treatment of Swiss 3T3 cells, which is consistent with the deamidation of these Gα subunits. Surprisingly, PMT also induced a similar modification of Gα11, a member of the Gq family of G-proteins that is not activated by PMT. Furthermore, an alkaline change in the isoelectric point of Gα13 was observed following PMT treatment of cells, suggesting differential modification of this Gα subunit by PMT. Gs was not affected by PMT treatment. Prolonged treatment with PMT led to a reduction in membrane-associated Gαi, but not Gαq. We also show that PMT inhibits the GTPase activity of Gq.

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Section: Discussionmentioning

confidence: 99%

Modification of Heterotrimeric G-Proteins in Swiss 3T3 Cells Stimulated with Pasteurella multocida Toxin

et al. 2012

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“…19 Its effect on dough is similar to that of traditional oxidizing improvers, hypothesized to act via the formation of disulfide crosslinks. 20 TG helps to strengthen the protein network, thereby modifying the rheological and baking properties of flour.…”

Section: Introductionmentioning

confidence: 89%

Effects of phenolic acids and transglutaminase on soft wheat flour dough and baked products

Koh

2008

J Sci Food Agric

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BACKGROUND: The effects of phenolic acids on the physical properties of soft wheat flour dough and baked soft wheat flour products were investigated. Transglutaminase (TG) was added to observe the effects of non-disulfide crosslinks on phenolic acid treated dough. Ferulic acid, p-coumaric acid or fumaric acid was blended with pastry flour at a level of 250, 500 or 1000 ppm of flour dry weight, respectively.

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“…First, the chemical nature of the cross-link formed in fibrin (Laki and Lorand, Science 1948) by blood coagulation factor XIIIa, a plasma transglutaminase (Loewy 1968), was revealed (Pisano et al 1968;Matatic and Loewy 1968;Lorand et al 1968). Second, the purification of tissue transglutaminase (later named transglutaminase 2; TG2) from guinea pig liver could be achieved (Folk and Cole 1966) in the NIH laboratory of Jack Folk, opening the way to the characterization of its enzymatic properties in details; the findings were summarized in the early seventies by Folk and Chung providing a basis of further developments in the field (Folk and Chung 1973).…”

Section: Introductionmentioning

confidence: 99%

Polymorphism of transglutaminase 2: unusually low frequency of genomic variants with deficient functions

2011

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Transglutaminase 2 (TG2) is a multifunctional member of an enzyme family: it modifies glutamine residues by cross-linking proteins and incorporating primary amines into them, has protein disulphide isomerase and protein kinase activities, mediates trans-membrane signal transduction and interactions between cell surface proteins and the extracellular matrix. These unusual multiple roles encoded into one polypeptide chain suggest that genomic variations in the TGM2 gene should be limited. Indeed, the available information in databases shows that unlike in the case of most other transglutaminases there are no common single nucleotide polymorphisms in exons of human TGM2. We collected data on and produced some of the rare genetic variants of TGM2 by site directed mutagenesis and found that some were less stable than the most abundant (wild type) enzyme variant and the majority had deficient transamidating activity. Further studies are required to clarify the pathologic significance of these rare TGM2 alleles in the human population.

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Molecular and Catalytic Properties of Transglutaminases

Cited by 115 publications

References 81 publications

Modification of Heterotrimeric G-Proteins in Swiss 3T3 Cells Stimulated with Pasteurella multocida Toxin

Modification of Heterotrimeric G-Proteins in Swiss 3T3 Cells Stimulated with Pasteurella multocida Toxin

Effects of phenolic acids and transglutaminase on soft wheat flour dough and baked products

Polymorphism of transglutaminase 2: unusually low frequency of genomic variants with deficient functions

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