CATH Classification

Domain Context

CATH Clusters

Superfamily Trypsin-like serine proteases
Functional Family Kallikrein 1-related peptidase C9

Enzyme Information

3.4.21.35
Tissue kallikrein.
based on mapping to UniProt P20151
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 (1)

P20151
KLK2_HUMAN
Homo sapiens
Kallikrein-2

PDB Structure

PDB 4NFF
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity
Skala, W., Utzschneider, D.T., Magdolen, V., Debela, M., Guo, S., Craik, C.S., Brandstetter, H., Goettig, P.
J.Biol.Chem.