CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.10 | Thrombin, subunit H |
|
2.40.10.10 | Trypsin-like serine proteases |
Domain Context
CATH Clusters
| Superfamily | Trypsin-like serine proteases |
| Functional Family | Kallikrein 8 (Neuropsin/ovasin) |
Enzyme Information
| 3.4.21.118 |
Kallikrein 8.
based on mapping to UniProt O60259
Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys.
-!- Activated by removal of an N-terminal prepropeptide. -!- The highest amidolytic activity is observed using Boc-Val-Pro- Arg-|-7-amido-4-methylcoumarin, which is a substrate of alpha- thrombin. -!- Substrates lacking basic amino acids in the P1 position are not cleaved. -!- Degrades casein, fibronectin, gelatin, collagen type IV, fibrinogen, and high-molecular-mass kininogen and is associated with diseases such as ovarian cancer and Alzheimer's disease. -!- Belongs to peptidase family S1A.
|
UniProtKB Entries (1)
| O60259 |
KLK8_HUMAN
Homo sapiens
Kallikrein-8
|
PDB Structure
| PDB | 5MS4 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural determinants of specificity and regulation of activity in the allosteric loop network of human KLK8/neuropsin.
Sci Rep
|
