CATH Classification

Domain Context

CATH Clusters

Superfamily Trypsin-like serine proteases
Functional Family kallikrein-6 isoform X2

Enzyme Information

3.4.21.118
Kallikrein 8.
based on mapping to UniProt Q61955
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)

Q61955
KLK8_MOUSE
Mus musculus
Kallikrein-8

PDB Structure

PDB 1NPM
External Links
Method X-RAY DIFFRACTION
Organism Spodoptera
Primary Citation
Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis.
Kishi, T., Kato, M., Shimizu, T., Kato, K., Matsumoto, K., Yoshida, S., Shiosaka, S., Hakoshima, T.
J.Biol.Chem.