Procollagen C-endopeptidase
| Procollagen C-endopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.19 | ||||||||
| CAS no. | 68651-95-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Procollagen C-endopeptidase (EC 3.4.24.19, procollagen C-terminal proteinase, carboxyprocollagen peptidase, procollagen C-terminal peptidase, procollagen C-proteinase, procollagen carboxypeptidase, procollagen carboxy-terminal proteinase, procollagen peptidase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Cleavage of the C-terminal propeptide at Ala-Asp in type I and II procollagens and at Arg-Asp in type III
This endopeptidase belongs to the peptidase family M12 (astacin family).
References
[edit]- ^ Hojima Y, van der Rest M, Prockop DJ (December 1985). "Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization". The Journal of Biological Chemistry. 260 (29): 15996–6003. PMID 3905801.
- ^ Kessler E, Adar R (December 1989). "Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55-kDa enhancer glycoprotein". European Journal of Biochemistry. 186 (1–2): 115–21. doi:10.1111/j.1432-1033.1989.tb15184.x. PMID 2689170.
External links
[edit]- Procollagen+C-endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
