The Structural Basis for Catalysis and Specificity of the X-Prolyl Dipeptidyl Aminopeptidase from Lactococcus lactis - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Structure Année : 2002

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

Résumé

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.

Dates et versions

hal-03351264 , version 1 (22-09-2021)

Identifiants

Citer

Pascal Rigolet, Ingrid Mechin, Marie-Madeleine Delage, Jean-Franç Ois Chich. The Structural Basis for Catalysis and Specificity of the X-Prolyl Dipeptidyl Aminopeptidase from Lactococcus lactis. Structure, 2002, pp.1383-1394. ⟨10.1016/s0969-2126(02)00851-1⟩. ⟨hal-03351264⟩
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