The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis.

Abstract

The X-prolyl dipeptidyl aminopeptidase (X-PDAP) from Lactococcus lactis is a dimeric enzyme catalyzing the removal of Xaa-Pro dipeptides from the N terminus of peptides. The structure of the enzyme was solved at 2.2 A resolution and provides a model for the peptidase family S15. Each monomer is composed of four domains. The larger one presents an alpha/beta… (More)

Topics

Cite this paper

@article{Rigolet2002TheSB, title={The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis.}, author={Pascal Rigolet and Ingrid Mechin and Marie-Madeleine Delage and J F Chich}, journal={Structure}, year={2002}, volume={10 10}, pages={1383-94} }