Investigation of a role for Glu-331 and Glu-305 in substrate binding of tripeptidyl-peptidase II.

@article{Linds2008InvestigationOA,
  title={Investigation of a role for Glu-331 and Glu-305 in substrate binding of tripeptidyl-peptidase II.},
  author={Anitra Lind{\aa}s and Sandra Eriksson and Emese Jozsa and Birgitta Tomkinson},
  journal={Biochimica et biophysica acta},
  year={2008},
  volume={1784 12},
  pages={
          1899-907
        }
}
The aim of this study was to investigate the mechanism by which tripeptidyl-peptidase II (TPP II) can specifically release tripeptides from the free N-terminus of an oligopeptide. The subtilisin-like N-terminal part of TPP II was modelled using subtilisin as template. Two glutamate residues (Glu-305 and Glu-331) appeared to be positioned so as to interact with the positively charged N-terminus of the substrate. In order to test this potential interaction, both residues were replaced by… CONTINUE READING
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