The Structural Basis for Catalysis and Specificity of the X-Prolyl Dipeptidyl Aminopeptidase from Lactococcus lactis

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Rigolet, Pascal | Mechin, Ingrid | Delage, Marie-Madeleine | Chich, Jean-Franç Ois

Edité par CCSD ; Elsevier (Cell Press) -

International audience. 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 hydrolase fold and comprises the active site serine. The specificity pocket is mainly built by residues from a small helical domain which is, together with the N-terminal domain, essential for dimerization. A C-terminal moiety probably plays a role in the tropism of X-PDAP toward the cellular membrane. These results give new insights for further exploration of the role of the enzymes of the SC clan.

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