Function and Biology Details
Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin B
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 27.49 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Length: 253 amino acids
Theoretical weight: 27.49 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P07688 (Residues: 80-332; Coverage: 80%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
