EC Number   |
General Information |
Reference |
|---|
   3.4.21.50 | evolution |
the enzyme belongs to the family of serine proteases |
732899 |
| 3.4.21.50 | more |
the additional disulfide bond (Cys6-Cys216) in the structure of lysyl endopeptidases, compared to trypsin, is thought to be responsible for their optimum activity at basic pH-values, 8.5-10.7, and their high resistance to denaturants |
732899 |
| 3.4.21.50 | more |
the enzyme has a hemagglutininadhesin domain in the polypeptide region C-terminal to the catalytic domains, three-dimensional crystal structure of enzyme Kgp. The conserved acidic residue Asp388 may play a role in the catalytic mechanism. A chain of three welldefined water molecules that acts as H-bond acceptors in their interactions with the Nf of the lysine. The other end of this H-bonded chain of water molecules is in turn H-bonded to the backbone carbonyl oxygen of Asp516, structure-function analysis, overview |
-, 732885 |
| 3.4.21.50 | physiological function |
characterisation of pepsin-solubilised collagen from the skin of unicorn leatherjacket Aluterus monocerous by lysyl endopeptidase |
708559 |
| 3.4.21.50 | physiological function |
gingipains, the principle virulence factors of Porphyromonas gingivalis are multidomain, cell-surface proteins containing a cysteine protease domain. The lysine specific gingipain, Kgp, is a critical virulence factor of Porphyromonas gingivalis |
-, 732885 |
