CATH Classification
Level | CATH Code | Description |
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2 | Mainly Beta |
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2.40 | Beta Barrel |
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2.40.10 | Thrombin, subunit H |
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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.
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UniProtKB Entries (1)
P00752 |
KLK_PIG
Sus scrofa
Glandular kallikrein
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PDB Structure
PDB | 2PKA |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Refined 2 A X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. Crystallization, structure determination, crystallographic refinement, structure and its comparison with bovine trypsin.
J.Mol.Biol.
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