The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: dipeptidyl-peptidase I
Reaction: Release of an N-terminal dipeptide, Xaa-Yaa┼Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro
Other name(s): cathepsin C; dipeptidyl aminopeptidase I; dipeptidyl transferase; dipeptide arylamidase I; DAP I
Comments: A Cl--dependent, lysosomal cysteine-type peptidase maximally active at acidic pH. Also polymerizes dipeptide amides, arylamides and esters at neutral pH. In peptidase family C1 (papain family).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9032-68-2
1.  Planta, R.J., Gorter, J. and Gruber, M. The catalytic properties of cathepsin C. Biochim. Biophys. Acta 89 (1964) 511–519. [PMID: 14209333]
2.  Metrione, R.M., Neves, A.G. and Fruton, J.S. Purification and properties of dipeptidyl transferase (cathepsin C). Biochemistry 5 (1966) 1597–1604. [PMID: 5961281]
3.  McDonald, J.K., Zeitman, B.B., Reilly, T.J. and Ellis, S. 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 (1969) 2693–2709. [PMID: 4306035]
4.  McDonald, J.K. and Schwabe, C. Intracellular exopeptidases. In: Barrett, A.J. (Ed.), Proteinases in Mammalian Cells and Tissues, North-Holland Publishing Co., Amsterdam, 1977, pp. 311–391.
[EC created 1961 as EC, transferred 1972 to EC]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald