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PEDS Advance Access originally published online on October 22, 2009
Protein Engineering Design and Selection 2009 22(12):747-752; doi:10.1093/protein/gzp061
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© The Author 2009. Published by Oxford University Press
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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

Uno Tagami1, Nobuhisa Shimba1,3, Mina Nakamura1, Kei-ichi Yokoyama1, Ei-ichiro Suzuki1 and Takatsugu Hirokawa2,3

1 Institute of Life Sciences, Ajinomoto Co., Inc, 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki-shi 210-8681, Japan 2Computational Biology Research Center (CBRC), National Institute of Advanced Industrial Science and Technology (AIST), 2-43-17F Aomi, Koutou-ku, Tokyo 135-0064, Japan

3 To whom correspondence should be addressed. E-mail: nobuhisa_shimba{at}ajinomoto.com (N.S.); E-mail: t-hirokawa{at}aist.go.jp (T.H.)

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.

Keywords: molecular dynamics/site-directed mutagenesis/substrate docking/substrate specificity/transglutaminase

Received June 30, 2009; revised August 30, 2009; accepted September 23, 2009.


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