EC Number |
Reaction |
Reference |
---|
3.4.21.35 | Preferential cleavage of Arg-/- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-/- or Leu-/-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-/- bonds |
S1 subsite accepts both Arg and Phe and has a preference for basic residues |
647514 |
3.4.21.35 | Preferential cleavage of Arg-/- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-/- or Leu-/-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-/- bonds |
serine at position P1' and arginine at position P2' result in high activity |
647489 |
3.4.21.35 | Preferential cleavage of Arg-/- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-/- or Leu-/-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-/- bonds |
strict preference for Arg in P1 position, wich is further enhanced by Ser in P1' position |
647542 |
3.4.21.35 | Preferential cleavage of Arg-/- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-/- or Leu-/-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-/- bonds |
substrate binding pocket contains an Asp residue |
647332 |
3.4.21.35 | Preferential cleavage of Arg-/- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-/- or Leu-/-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-/- bonds |
trypsin-like serine protease |
647332 |