Dipeptidyl-peptidase I

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Dipeptidyl peptidase I
Cathepsin C, heterododekamer, Human
EC no.
CAS no.9032-68-2
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

Dipeptidyl peptidase I (EC, cathepsin C, dipeptidyl aminopeptidase I, dipeptidyl transferase, dipeptide arylamidase I, DAP I) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Release of an N-terminal dipeptide, Xaa-Yaa!Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro

This Cl-dependent, lysosomal cysteine-type peptidase is maximally active at acidic pH.


  1. ^ Planta RJ, Gorter J, Gruber M (September 1964). "The catalytic properties of cathepsin C". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 89 (3): 511–9. doi:10.1016/0926-6569(64)90077-x. PMID 14209333.
  2. ^ Metroione RM, Neves AG, Fruton JS (May 1966). "Purification and properties of dipeptidyl transferase (Cathepsin C)". Biochemistry. 5 (5): 1597–604. doi:10.1021/bi00869a021. PMID 5961281.
  3. ^ McDonald JK, Zeitman BB, Reilly TJ, Ellis S (May 1969). "New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). Including the degradation of beta-corticotropin and other peptide hormones". The Journal of Biological Chemistry. 244 (10): 2693–709. PMID 4306035.
  4. ^ McDonald, J.K.; Schwabe, C. (1977). "Intracellular exopeptidases". In Barrett, A.J. (ed.). Proteinases in Mammalian Cells and Tissues. Amsterdam: North-Holland Publishing Co. pp. 311–391.

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