S28 peptidases: lessons from a seemingly 'dysfunctional' family of two

BMC Biol. 2010 Jun 28:8:87. doi: 10.1186/1741-7007-8-87.

Abstract

A recent paper in BMC Structural Biology reports the crystal structure of human prolylcarboxypeptidase (PRCP), one of the two members of the S28 peptidase family. Comparison of the substrate-binding site of PRCP with that of its family partner, dipeptidyl dipeptidase 7 (DPP7), helps to explain the different enzymatic activities of these structurally similar proteins, and also reveals a novel apparent charge-relay system in PRCP involving the active-site catalytic histidine. See research article: http://www.biomedcentral.com/1472-6807/10/16/

Publication types

  • Comparative Study

MeSH terms

  • Carboxypeptidases / genetics*
  • Carboxypeptidases / metabolism
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / genetics*
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / metabolism
  • Humans
  • Models, Molecular*
  • Multigene Family / genetics*
  • Protein Conformation
  • Substrate Specificity

Substances

  • Carboxypeptidases
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • dipeptidyl peptidase II
  • lysosomal Pro-X carboxypeptidase