Enteropeptidase
| Enteropeptidase | ||
|---|---|---|
|
||
| Band model according to PDB 1EKB | ||
| Properties of human protein | ||
| Mass / length primary structure | 1019 = 784 + 235 amino acids | |
| Secondary to quaternary structure | Heterodimer | |
| Identifier | ||
| Gene names | PRSS7 ; ENTK | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 3.4.21.9 , serine protease | |
| MEROPS | S01.156 | |
| Response type | hydrolysis | |
| Substrate | Trypsinogen | |
| Products | Trypsin + hexapeptide (Val- [Asp] 4 -Lys) |
|
| Occurrence | ||
| Homology family | PRSS7 | |
| Parent taxon | Euteleostomi | |
Enteropeptidase or (out of date and misleading according to biochemical nomenclature, since the enzyme does not catalyze phosphorylation) enterokinase , is an enzyme in the brush border of vertebrates , which is formed by the duodenal mucosa . By splitting off a hexapeptide (Val- [Asp] 4 -Lys), the membrane-bound enteropeptidase converts the inactive proenzyme trypsinogen into its active form trypsin , which indirectly activates other enzymes in the pancreatic secretion.
Enteropeptidase catalyzes the following reaction:
- Trypsinogen → trypsin + hexapeptide
swell
- Roche , Lexicon of Medicine, 5th edition (http://www.tk-online.de/rochelexikon/)
- Robert F. Schmidt, Florian Lang: Human physiology with pathophysiology; Springer Medizin Verlag, Heidelberg, 30th edition 2007