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 |
Enzyme Information
| 3.4.21.35 |
Tissue kallikrein.
based on mapping to UniProt P00752
Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.
-!- Formed from tissue prokallikrein by activation with trypsin. -!- A large number of tissue kallikrein-related sequences have been reported for rats and mice, though fewer seem to exist in other mammals. -!- The few that have been isolated and tested on substrates include mouse EC 3.4.21.54, submandibular proteinase a, epidermal growth- factor-binding protein, nerve growth factor gamma-subunit, rat tonin, submaxillary proteinases A and B, T-kininogenase, kallikreins K7 and K8. -!- The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-|-Xaa bonds. -!- Belongs to peptidase family S1. -!- Formerly EC 3.4.21.8.
|
UniProtKB Entries (2)
| P00752 |
KLK_PIG
Sus scrofa
Glandular kallikrein
|
| P80302 |
ANTA_HIRME
Hirudo medicinalis
Hirustasin
|
PDB Structure
| PDB | 1HIA |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex.
Structure
|