Transglutaminase 2

We report the constitution and molecular characterization of a novel transglutaminase (EC 2.3.2.13) that starts to accumulate speci®cally in thenucleus in the star®sh (Asterina pectinifera) embryo after progression through the early blastula stage. The cDNA for the nuclear transglutaminase was clonedand the cDNA-deduced sequence de®nes a single open reading frame encoding aproteinwith737 aminoacids andapredictedmolecularmass of 83 kDa.

11p research12 23-04-2013 49 3   Download

Streptomyces mobaraensis secretes a Ca 2+ -independent transglutaminase (TGase) that is activated by removing an N-terminal peptide from a precursor protein during sub-merged culture in a complex medium [Pasternack, R., Dorsch, S., Otterbach, J. T., Robenek, I. R., Wolf, S. & Fuchsbauer, H.-L. (1998)Eur. J. Biochem. 257, 570–576]. However, an activating protease could not be identified, probably because of the presence of a 14-kDa protein (P14 ) belonging to theStreptomycessubtilisin inhibitor family. ...

9p tumor12 20-04-2013 32 2   Download

Transglutaminases form a large family of intracellular and extracellular enzymes that catalyse the Ca 2+ -dependent post-translational modification of proteins. Despite significant advances in our understanding of the biolo-gical role of most mammalian transglutaminase isoforms, recent findings suggest new scenarios, most notably for the ubiquitous tissue transglutami-nase.

17p awards 05-04-2013 45 3   Download

Transglutaminases are Ca 2+ -dependent enzymes that post-translationally modify proteins by crosslinking or polyamination at specific polypeptide-bound glutamine residues.Physarum polycephalum, an acellular slime mold, is the evolutionarily lowest organism expressing a transglutimase whose primary structure is similar to that of mammalian transglutimases.

12p galaxyss3 19-03-2013 35 3   Download

The multifunctional tissue transglutaminase 2 (TG2) has a four-domain structure with several Ca 2+ -regulated biochemical activities, including transglutamylation and GTP hydrolysis. The structure of the Ca 2+ -binding form of the human enzyme is not known, and its Ca 2+ -binding sites have not been fully characterized.

14p vinaphone15 25-02-2013 33 3   Download

Transglutaminase 2 (TG2; EC 2.3.2.13) is the most abundantly expressed member of the transglutaminase family and exerts opposing effects on cell growth, differentiation and apoptosis via multiple activities, including transamidase, GTPase, cell adhesion, protein disulfide isomerase, kinase and scaffold activities.

12p cosis54 08-12-2012 38 2   Download

Tissue transglutaminase (TG2) is a ubiquitously expressed member of the transglutaminase family of Ca 2+ -dependent crosslinking enzymes. Unlike other family members, TG2 is a multifunctional protein, which has several other well documented enzymatic and non-enzymatic functions.

13p cosis54 08-12-2012 44 2   Download