Tripeptidyl peptidase II

Tripeptidyl peptidase II (TPP II) is a proteolytic enzyme that plays a crucial role in the degradation of intracellular proteins. It is a member of the serine protease family and is primarily found in the cytoplasm of eukaryotic cells. TPP II is involved in the breakdown of peptides into smaller amino acid fragments, which can then be utilized for various cellular processes.

Function

TPP II is responsible for the hydrolysis of tripeptides from the N-terminus of proteins. It cleaves the peptide bond between the second and third amino acids, releasing dipeptides and free amino acids. This process is essential for the recycling of amino acids and the maintenance of cellular homeostasis.

Structure

TPP II is a large, multi-domain protein consisting of several distinct regions. It contains an N-terminal proline-rich domain, a central catalytic domain, and a C-terminal domain. The catalytic domain is responsible for the enzymatic activity of TPP II, while the other domains are involved in protein-protein interactions and regulation.

Role in Disease

TPP II has been implicated in various disease processes. Studies have shown that dysregulation of TPP II activity can lead to the accumulation of abnormal peptides and proteins, which can contribute to the development of neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease. Additionally, TPP II has been found to be overexpressed in certain types of cancer, suggesting its potential as a therapeutic target.

Clinical Applications

Due to its involvement in disease processes, TPP II has garnered interest as a potential target for therapeutic interventions. Inhibitors of TPP II have been developed and tested for their efficacy in treating neurodegenerative diseases and cancer. These inhibitors work by blocking the enzymatic activity of TPP II, thereby preventing the degradation of abnormal peptides and proteins.

References

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See Also

• Proteolysis
• Serine protease
• Neurodegenerative diseases
• Cancer