Search results
Results from the WOW.Com Content Network
Transglutaminase 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.
Transglutaminase 2 (TG2) is a ubiquitously expressed (intracellular as well as extracellular) protein, with multiple modes of Post-translational regulation, including an allosteric disulfide bond between Cys-370-Cys-371 that renders the enzyme inactive in the extracellular matrix.
Factor XIII is a transglutaminase that circulates in human blood as a heterotetramer of two A and two B subunits. Factor XIII binds to the clot via their B units. In the presence of fibrins, thrombin efficiently cleaves the R37–G38 peptide bond of each A unit within a XIII tetramer.
While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene consists of two polypeptide chains activated from a single precursor protein by proteolysis.
Tissue factor, FV and FVIII are glycoproteins, and Factor XIII is a transglutaminase. [27] The coagulation factors circulate as inactive zymogens. The coagulation cascade is therefore classically divided into three pathways. The tissue factor and contact activation pathways both activate the "final common pathway" of factor X, thrombin and ...
The structure of glutaminase has been determined using X-ray diffraction to a resolution of up to 1.73 Å. There are 2 chains containing 305 residues that make up the length of this dimeric protein. On each strand, 23% of the amino acid content, or 71 residues, are found in the 8 helices.
TGM5 is a transglutaminase enzyme.. TGM5 encodes one member of the multigene transglutaminase family. Transglutaminases (TGs) are involved in protein cross-linking by catalyzing the formation of gamma-glutamyl-lysine isodipeptide bonds between adjacent polypeptides (Candi et al. 2005; Eckert et al. 2005).
A deficiency is associated with ichthyosis lamellaris. [11] Epidermal transglutaminase is the autoantigen, in humans, of dermatitis herpetiformis.. A study on the mutation of keratinocyte transglutaminase (TGK) came to conclude that those affected with ichthyosis lamellaris, present a substantial deficit in keratinocyte transglutaminase activity. [8]