Dipeptidyl-peptidase II

Enzyme

Dipeptidyl-peptidase II

Dipeptidyl-peptidase II (DPP II) is an enzyme that belongs to the class of proteases, specifically the serine proteases. It is involved in the cleavage of dipeptides from the N-terminus of polypeptides. This enzyme is also known as quiescent cell proline dipeptidase.

Function

Dipeptidyl-peptidase II plays a crucial role in the degradation of proline-containing peptides. It is involved in various physiological processes, including the regulation of hormones and neuropeptides. DPP II is known to be active in lysosomes and is implicated in the processing of antigens for immune responses.

Structure

Dipeptidyl-peptidase II is a homodimeric enzyme, meaning it consists of two identical subunits. Each subunit contains an active site that is responsible for its enzymatic activity. The enzyme's structure allows it to specifically recognize and cleave dipeptides from the N-terminus of substrates.

Mechanism

The enzymatic activity of Dipeptidyl-peptidase II involves the hydrolysis of peptide bonds. The enzyme utilizes a serine residue in its active site to perform nucleophilic attack on the peptide bond, leading to the release of a dipeptide. This mechanism is characteristic of serine proteases.

Clinical Significance

Alterations in the activity of Dipeptidyl-peptidase II have been associated with various diseases. For instance, abnormal DPP II activity has been linked to certain types of cancer and immune disorders. Understanding the function and regulation of this enzyme can provide insights into potential therapeutic targets.

Related Enzymes

Dipeptidyl-peptidase II is part of a larger family of dipeptidyl peptidases, which includes:

• Dipeptidyl peptidase-4 (DPP-4)
• Dipeptidyl peptidase-8 (DPP-8)
• Dipeptidyl peptidase-9 (DPP-9)

See Also

• Protease
• Serine protease
• Lysosome
• Antigen processing

References

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