EC Number   |
General Information |
Reference |
|---|
   2.3.2.13 | evolution |
as a member of the transglutaminase family, transglutaminase 2 (TG2) can catalyze deamidation or alternatively transamidation of selected Gln residues in proteins and peptides. Redox regulation unique to TG2 and evolved relatively recently, TG2 homologues in other vertebrates appear to lack this structure feature |
758635 |
| 2.3.2.13 | evolution |
crayfish TGase is adapted to have significant activity at low temperatures since crayfish are living in quite cold waters |
759209 |
| 2.3.2.13 | evolution |
transglutaminase 2 (TG2) is a ubiquitously expressed multifunctional member of the transglutaminase enzyme family |
758750 |
| 2.3.2.13 | evolution |
transglutaminase is an enzyme family responsible for post-translational modification such as protein cross-linking and the attachment of primary amine and/or deamidation of glutamine-residue in proteins. The medaka orthologue of human tissue-type transglutaminase (OlTGT), identified in the established model fish, has similar functions compared to mammalian enzyme |
758933 |
| 2.3.2.13 | malfunction |
double-TG1/TG2 knockout mice show epidermal features similar to TG1 knockout mice. Double-FXIII-A/TG2 knockout mice exhibit only a transient delay in bone mineral density and growth relative to wild-type mice |
759166 |
| 2.3.2.13 | malfunction |
effective inhibition of renal interstitial fibrosis by TG inhibitors but only partial reduction of fibrosis in TG2 knockout mice |
759166 |
| 2.3.2.13 | malfunction |
enzyme inactivation significantly reduces the virulence of Streptococcus suis serotype 2 in a pig infection model and impairs its antiphagocytosis in human blood |
736480 |
| 2.3.2.13 | malfunction |
failure in the regulation of TG2 activities is associated with many human diseases, including inflammatory disease, celiac disease, neurodegenerative disease, diabetes, tissue fibrosis, and cancers. Comparison of wild-type with G224V mutant enzyme structrue and actives sites, overview. Since the active site cysteine (C277)-containing alpha-helix, whose location may be important for TG2 activity, is interacted with a neighboring intramolecular alpha-helix, which contains residue 224, replacement of G with V will have an effect on the transamidase activity of TG2. Decreased activity of G224 may be due to the higher chance of location shift on active site cysteine (C277) because of the loss of the hydrophobic cluster anchored by V224 |
760040 |
| 2.3.2.13 | malfunction |
loss of TG1 and TG5 cross linking leads to defects in epidermal cornification in lamellar ichthyosis and acral peeling skin syndrome, respectively. Homozygous missense mutations in the gene encoding TG5 are found to correlate with acral peeling skin syndrome, which is characterized by continual shedding of the outer epidermis of the dorsa of the hands and feet from birth and throughout life |
759166 |
| 2.3.2.13 | malfunction |
loss of TG1 and TG5 cross linking leads to defects in epidermal cornification in lamellar ichthyosis and acral peeling skin syndrome, respectively. Lamellar ichthyosis is apparent at birth, with newborns encased in a shiny, waxy layer of skin (collodion babies) that sheds to reveal scaling and shedding of the outer epidermis and a severely compromised skin barrier. It is an autosomal-recessive disease, with mutations in the gene encoding TG1 accounting for about 90% of cases. Lamellar ichthyosis is an orphan disease. TG1 and TG2 are the most abundantly expressed TGs in normal kidney, and renal disease progression correlates with increases in activity of intracellular TG1 in renal tubular epithelium and of TG2 in the extracellular matrix |
759166 |
