IUBMB Enzyme Nomenclature

EC 3.4.14.1

Accepted name: dipeptidyl-peptidase I

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

Other names: cathepsin C; dipeptidyl aminopeptidase I; dipeptidyl transferase; cathepsin C; 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). Formerly EC 3.4.4.9

Links to other databases: BRENDA, EXPASY, KEGG, GTD, MEROPS, Metacyc, PDB, CAS registry number: 9032-68-2

References

1. Planta, R.J., Gorter, J. and Gruber, M. The catalytic properties of cathepsin C. Biochim. Biophys. Acta 89 (1964) 511-519

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 Proteinases in Mammalian Cells and Tissues (Barrett, A.J. ed.), pp. 311-391 (1977) North-Holland Publishing Co, Amsterdam

[EC 3.4.14.1 created 1961 as EC 3.4.4.9, transferred 1972 to EC 3.4.14.1]


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