Dipeptidyl-peptidase II

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Enzyme


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Identifiers
EC number3.4.14.2
CAS number37288-70-7
Alt. names
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway



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[edit | edit source]

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[edit | edit source]

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[edit | edit source]

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[edit | edit source]

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[edit | edit source]

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

See Also[edit | edit source]

References[edit | edit source]

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Contributors: Prab R. Tumpati, MD