| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10762789 | Biochemical and Biophysical Research Communications | 2011 | 6 Pages |
Abstract
⺠The E312/E343 double-Glu motif of tripeptidylpeptidase II is highly asymmetrical. ⺠E312 both blocks the active-site cleft at position P4 and acts as the prime docking residue. ⺠A salt bridge involving E312 conveys high exopeptidase selectivity. ⺠Substrate binding to the prime-site subsites enables weak endopeptidolysis.
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Authors
Jürgen Peters, Anne-Marie Schönegge, Beate Rockel, Wolfgang Baumeister,