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Protein Engineering, Design and Selection

Year: 2009  |  Volume: 22  |  Issue: 12  |  Page No.: 747 - 752

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

U Tagami, N Shimba, M Nakamura, K. i Yokoyama, E. i Suzuki and T. Hirokawa


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.

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