Pancreatic endopeptidase E
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 | ||||||||
|
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
This enzyme is peptidase of family S1 (trypsin family) from pancreatic juice.
References
- ↑ Mallory, P.A.; Travis, J. (1975). "Human pancreatic enzymes: purification and characterization of a nonelastolytic enzyme, protease E, resembling elastase". Biochemistry. 14 (4): 722–729. doi:10.1021/bi00675a012. PMID 234742.
- ↑ Shen, W.; Fletcher, T.S.; Largman, C. (1987). "Primary structure of human pancreatic protease E determined by sequence analysis of the cloned mRNA". Biochemistry. 26: 3447–3452. 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 - version of the 5/22/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.