Dipeptidyl-peptidase I

Dipeptidyl peptidase I
Identifiers
EC number 3.4.14.1
CAS number 9032-68-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Dipeptidyl peptidase I (EC 3.4.14.1, 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.

References

  1. Planta, R.J., Gorter, J. and Gruber, M. (1964). "The catalytic properties of cathepsin C". Biochim. Biophys. Acta 89: 511–519. doi:10.1016/0926-6569(64)90077-x. PMID 14209333.
  2. Metrione, R.M., Neves, A.G. and Fruton, J.S. (1966). "Purification and properties of dipeptidyl transferase (cathepsin C)". Biochemistry 5: 1597–1604. doi:10.1021/bi00869a021. PMID 5961281.
  3. McDonald, J.K., Zeitman, B.B., Reilly, T.J. and Ellis, S. (1969). "New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I) including the degradation of β-corticotropin and other peptide hormones". J. Biol. Chem. 244: 2693–2709. PMID 4306035.
  4. McDonald, J.K. and Schwabe, C. (1977). "Intracellular exopeptidases". In Barrett, A.J. Proteinases in Mammalian Cells and Tissues. Amsterdam: North-Holland Publishing Co. pp. 311–391.

External links

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