Function and Biology Details
Reaction catalysed:
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 (5).
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assemblies composition:
Assembly name:
Glandular kallikrein (preferred)
PDBe Complex ID:
PDB-CPX-133312 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glandular kallikrein
Molecule details ›
Chains: A, X
Length: 80 amino acids
Theoretical weight: 9.12 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 80 amino acids
Theoretical weight: 9.12 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
- Canonical:
P00752 (Residues: 8-87; Coverage: 33%)
Structure domains: Trypsin-like serine proteases
Glandular kallikrein
Molecule details ›
Chains: B, Y
Length: 152 amino acids
Theoretical weight: 16.51 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 152 amino acids
Theoretical weight: 16.51 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
- Canonical: P00752 (Residues: 95-148, 150-170, 172-174, 176-246; Coverage: 61%)
Structure domains: Trypsin-like serine proteases
