Defective α2antiplasmin cross-linking and thrombus stability in a case of acquired factor XIII deficiency

This work was supported by grants FS/11/2/28579 (N.J.M) and from the British Heart Foundation and by the University of Aberdeen Development Trust (J.L.M) and Friends of Anchor (N.J.M & J.L.M).Peer reviewedPostprin

Substrate specificity of microbial transglutaminase as revealed by three-dimensional docking simulation and mutagenesis

Transglutaminases (TGases) are used in fields such as food and pharmaceuticals. Unlike other TGases, microbial transglutaminase (MTG) activity is Ca2+-independent, broadening its application. Here, a three-dimensional docking model of MTG binding to a peptide substrate, CBZ-Gln-Gly, was simulated. The data reveal CBZ-Gln-Gly to be stretched along the MTG active site cleft with hydrophobic and/or aromatic residues interacting directly with the substrate. Moreover, an oxyanion binding site for TGase activity may be constructed from the amide groups of Cys64 and/or Val65. Alanine mutagenesis verified the simulated binding region and indicated that large molecules can be widely recognized on the MTG cleft