Post-proline-cleaving peptidases having DP IV like enzyme activity. Post-proline peptidases

Adv Exp Med Biol. 2000:477:103-9. doi: 10.1007/0-306-46826-3_10.

Abstract

DP IV has been studied extensively in disease and in the immune system by the use of enzyme assays which detect hydrolysis of Gly-Pro or Ala-Pro substrate. In addition many studies have used inhibitors of DP IV enzyme activity. The characterisation of a novel DP IV like protein, DPP4R, and of other proteases which have a substrate specificity similar to DP IV or that bind DP IV inhibitors suggests that these studies require further evaluation.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Animals
  • Dipeptidyl Peptidase 4 / metabolism*
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / chemistry
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / metabolism
  • Humans
  • Hydrolysis
  • Membrane Proteins / classification
  • Membrane Proteins / metabolism
  • Peptide Hydrolases / classification
  • Peptide Hydrolases / metabolism*
  • Proline / chemistry*
  • Protein Structure, Tertiary
  • Substrate Specificity
  • Swine

Substances

  • Membrane Proteins
  • Proline
  • Peptide Hydrolases
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • Dipeptidyl Peptidase 4