Pancreatic endopeptidase E
Pancreatic endopeptidase E (EC 3.4.21.70, cholesterol-binding proteinase, proteinase E, cholesterol-binding serine proteinase, pancreatic protease E, pancreatic proteinase E, cholesterol-binding pancreatic proteinase, CBPP, pancreas E proteinase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Preferential cleavage: Ala-. Does not hydrolyse elastin
| Pancreatic endopeptidase E | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.21.70 | ||||||||
| CAS number | 68073-27-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme is peptidase of family S1 (trypsin family) from pancreatic juice.
References
- Mallory PA, Travis J (February 1975). "Human pancreatic enzymes: purification and characterization of a nonelastolytic enzyme, protease E. resembling elastase". Biochemistry. 14 (4): 722–30. doi:10.1021/bi00675a012. PMID 234742.
- Shen WF, Fletcher TS, Largman C (June 1987). "Primary structure of human pancreatic protease E determined by sequence analysis of the cloned mRNA". Biochemistry. 26 (12): 3447–52. doi:10.1021/bi00386a030. PMID 3477287.
External links
- Pancreatic+endopeptidase+E at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.