| EC |
3.4.14.1 |
| 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, Gene, GTD, KEGG, MetaCyc, MEROPS, 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. [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. |
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| [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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