Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. This enzyme has a vasoconstrictor activity. KLK-9 has both a chymotrypsin-like and a trypsin-like properties. 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. Heterodimer of a light chain and heavy chain linked by a disulfide bond. Belongs to the peptidase S1 family. Kallikrein subfamily.