Dipeptidyl-peptidase II is related to lysosomal Pro-X carboxypeptidase

Biochim Biophys Acta. 1996 Nov 14;1298(1):1-3. doi: 10.1016/s0167-4838(96)00153-7.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carboxypeptidases / chemistry*
  • Carboxypeptidases / metabolism
  • Databases, Factual
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / chemistry*
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / metabolism
  • Lysosomes / enzymology*
  • Molecular Sequence Data
  • Proline / metabolism
  • Semen / enzymology
  • Sequence Alignment
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / metabolism
  • Software
  • Swine

Substances

  • Proline
  • Carboxypeptidases
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • dipeptidyl peptidase II
  • Serine Endopeptidases