Proteasomes exhibit catalytic activity by breaking down peptide bonds in proteins. The core particle of the proteasome, known as the 20S core, contains proteolytic sites that cleave peptide bonds. These sites have different specificities: chymotrypsin-like, trypsin-like, and caspase-like, allowing the proteasome to degrade a broad range of substrates. The catalytic activity of the proteasome is ATP-dependent, requiring energy to unfold and translocate proteins into the core for degradation.
