Membrane bound members of the M1 family: more than aminopeptidases

Protein Pept Lett. 2004 Oct;11(5):491-500. doi: 10.2174/0929866043406643.

Abstract

In mammals the M1 aminopeptidase family consists of nine different proteins, five of which are integral membrane proteins. The aminopeptidases are defined by two motifs in the catalytic domain; a zinc binding motif HEXXH-(X18)-E and an exopeptidase motif GXMEN. Aminopeptidases of this family are able to cleave a broad range of peptides down to only to a single peptide. This ability to either generate or degrade active peptide hormones is the focus of this review. In addition to their capacity to degrade a range of peptides a number of these aminopeptidases have novel functions that impact on cell signalling and will be discussed.

Publication types

  • Review

MeSH terms

  • Aminopeptidases / chemistry
  • Aminopeptidases / classification
  • Aminopeptidases / genetics
  • Aminopeptidases / metabolism*
  • Animals
  • CD13 Antigens / chemistry
  • CD13 Antigens / metabolism
  • Cystinyl Aminopeptidase
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / classification
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Minor Histocompatibility Antigens
  • Pyrrolidonecarboxylic Acid / analogs & derivatives*
  • Pyrrolidonecarboxylic Acid / chemistry
  • Pyrrolidonecarboxylic Acid / metabolism

Substances

  • Membrane Proteins
  • Minor Histocompatibility Antigens
  • Aminopeptidases
  • ERAP1 protein, human
  • CD13 Antigens
  • Cystinyl Aminopeptidase
  • leucyl-cystinyl aminopeptidase
  • pyroglutamyl-peptidase II
  • Pyrrolidonecarboxylic Acid