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

Protein Engineering, Design and Selection , Volume 22 (12): 747 – Dec 1, 2009

Details

Publisher
Oxford University Press
Copyright
Copyright © 2010 Oxford University Press
ISSN
1741-0126
eISSN
1741-0134
D.O.I.
10.1093/protein/gzp061
Publisher site
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Substrate specificity of microbial transglutaminase as revealed by three-dimensional docking simulation and mutagenesis

Abstract

Abstract Transglutaminases (TGases) are used in fields such as food and pharmaceuticals. Unlike other TGases, microbial transglutaminase (MTG) activity is Ca 2+ -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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