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By Andersen E.W.

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Some of them may be considered chemically similar although with differences in terms of substrate specificity and kinetic features. Most of these functions are present in TGase 2. This may reflect a real multifunctionality restricted to this isoenzyme only, but most probably this is simply due to the fact that TGase 2 is ubiquitous, heavily involved in cellular processes like apoptosis and differentiation, and in human diseases like celiac disease. Therefore it is not surprising that TGase 2 is the most studied and it is possible that other TGase isoenzymes, less studied, are multifunctional enzymes too.

The last ␣-helix (H4) harbors the residues homologous to the sole Ca2ϩ-binding site in factor XIIIa. The core and barrel 1 domains are connected by a flexible loop (amino acids 454–478) which might act as a hinge when barrel 1 releases the core domain to retrieve the latent transglutaminase activity. Barrel 1 comprises six ␤-strands and one ␤-turn, barrel 2 folds into seven antiparallel ␤-strands. Structural Correlates of Transglutamination Data from deletion studies revealed that the two barrel domains are not necessary for TGase activity – on the contrary, their loss increases catalytic rate – whereas the ␤-sandwich and the core domains are indispensable [22].

On the other hand, the hydrolysis of acetyl, ␣-alanyl- and ␥-glutamyl-p-nitrophenyl esters by guinea pig liver transglutaminase was routinely used in Jack Folk’s laboratory to compare kinetic parameters for amine substrates, as the better amine substrate resulted in a faster release of the nitrophenol chromogen [6]. These calculations subtracted the velocity of hydrolysis (as blank) from that of amine incorporation. 05–2 millimolar) concentrations [7]. The effective ratio between deamidated and transamidated glutamines under in vivo conditions may depend largely on the availability of amine substrates.

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