Dipeptidyl-peptidase II is related to lysosomal Pro-X carboxypeptidase.
The N-terminal amino-acid sequence of pig dipeptidyl-peptidase II (EC 3.4.14.2; DPP II) recently published (Huang, K., Takagaki, M., Kani, K. and Ohkubo, I. (1996) Biochim. Biophys. Acta 1290, 149-156) proves that the enzyme is homologous with lysosomal Pro-X carboxypeptidase (EC 3.4.16.2), and belongs to peptidase family S28 in clan SC. This is consistent with a number of biochemical similarities between these two prolyl bond-cleaving serine peptidases. DPP II is not related to granzymes, as was suggested by Huang et al.
Rawlings
N D
ND
Department of Immunology, Babraham Institute, Cambridge, UK.
Barrett
A J
AJ
D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases / Q000737:chemistry* / Q000378:metabolism; D016208:Databases, Factual; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000737:chemistry* / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology*; D008969:Molecular Sequence Data; D011392:Proline / Q000378:metabolism; D012661:Semen / Q000201:enzymology; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D012984:Software; D013552:Swine
D011392:Proline; D002268:Carboxypeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C100151:dipeptidyl peptidase II; D012697:Serine Endopeptidases