| EC |
3.4.23.5 |
| Accepted name: |
cathepsin D |
| Reaction: |
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the Gln4-His bond in B chain of insulin |
| Comments: |
Occurs intracellularly, in lysosomes. A zymogen form is known [4]. In peptidase family A1 (pepsin A family). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-26-7 |
| References: |
| 1. |
Barrett, A.J. Cathepsin D and other carboxyl proteinases. In: Barrett, A.J. (Ed.), Proteinases in Mammalian Cells and Tissues, North-Holland Publishing Co., Amsterdam, 1977, pp. 209–248. |
| 2. |
Takahashi, T. and Tang, J. Cathepsin D from porcine and bovine spleen. Methods Enzymol. 80 (1981) 565–581. [PMID: 7341918] |
| 3. |
Faust, P.L., Kornfeld, S. and Chirgwin, J.M. Cloning and sequence analysis of cDNA for human cathepsin D. Proc. Natl. Acad. Sci. USA 82 (1985) 4910–4914. [DOI] [PMID: 3927292] |
| 4. |
Conner, G.E. Isolation of procathepsin D from mature cathepsin D by pepstatin affinity chromatography. Autocatalytic proteolysis of the zymogen form of the enzyme. Biochem. J. 263 (1989) 601–604. [PMID: 2512908] |
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| [EC 3.4.23.5 created 1965 as EC 3.4.4.23, transferred 1972 to EC 3.4.23.5, modified 1986] |
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