Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism.

@article{Okada2007CrystalSO,
  title={Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism.},
  author={Toshihiro Okada and Hideyuki Suzuki and Kei Wada and Hidehiko Kumagai and Keiichi Fukuyama},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 4},
  pages={2433-9}
}
Gamma-glutamyltranspeptidase (GGT) is an extracellular enzyme that plays a key role in glutathione metabolism. The mature GGT is a heterodimer consisting of L- and S-subunits that is generated by posttranslational cleavage of the peptide bond between Gln-390 and Thr-391 in the precursor protein. Thr-391, which becomes the N-terminal residue of the S-subunit, acts as the active residue in the catalytic reaction. The crystal structure of a mutant GGT, T391A, that is unable to undergo… CONTINUE READING

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T. Okada, H. Suzuki, K. Wada, H. Kumagai, K. Fukuyama
Proc. Natl. Acad. Sci. by gest on Sptem er 16, • 2006

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