title: Post-proline-cleaving peptidases having DP IV like enzyme activity. Post-proline peptidases.
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.
authors.affiliation: A.W. Morrow Gastroenterology and Liver Centre, Royal Prince Alfred Hospital, NSW, Australia.
authors.forename: C A
authors.initials: CA
authors.lastname: Abbott
authors.forename: D
authors.initials: D
authors.lastname: Yu
authors.forename: G W
authors.initials: GW
authors.lastname: McCaughan
authors.forename: M D
authors.initials: MD
authors.lastname: Gorrell
mesh_terms: D000818:Animals; D018819:Dipeptidyl Peptidase 4 / Q000378:metabolism*; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D008565:Membrane Proteins / Q000145:classification / Q000378:metabolism; D010447:Peptide Hydrolases / Q000145:classification / Q000378:metabolism*; D011392:Proline / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D013552:Swine
chemical_list: D008565:Membrane Proteins; D011392:Proline; D010447:Peptide Hydrolases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D018819:Dipeptidyl Peptidase 4