Insulysin
Enzyme involved in insulin degradation
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Identifiers | |
---|---|
EC number | 3.4.24.56 |
CAS number | 160618-45-3 |
Alt. names | |
IntEnz | IntEnz view |
BRENDA | BRENDA entry |
ExPASy | NiceZyme view |
KEGG | KEGG entry |
MetaCyc | metabolic pathway |
Insulysin, also known as insulin-degrading enzyme (IDE), is a zinc-binding metalloprotease enzyme that plays a crucial role in the degradation of insulin and other small peptides. It is encoded by the IDE gene in humans.
Function[edit | edit source]
Insulysin is primarily involved in the catabolism of insulin, a hormone that regulates glucose levels in the blood. By degrading insulin, insulysin helps to maintain homeostasis of blood glucose levels. In addition to insulin, insulysin also degrades other peptides such as amyloid beta, which is implicated in Alzheimer's disease.
Structure[edit | edit source]
Insulysin is a member of the M16 family of metalloproteases and requires zinc for its enzymatic activity. The enzyme is composed of two homologous domains that form a large central cavity where substrate binding and catalysis occur.
Mechanism[edit | edit source]
The enzymatic activity of insulysin involves the binding of zinc at its active site, which is essential for the hydrolysis of peptide bonds. The enzyme recognizes and binds to specific sequences in its substrate peptides, facilitating their degradation.
Clinical Significance[edit | edit source]
Dysfunction or altered expression of insulysin has been linked to several diseases, including type 2 diabetes and Alzheimer's disease. In type 2 diabetes, reduced insulysin activity can lead to prolonged insulin action and impaired glucose regulation. In Alzheimer's disease, decreased degradation of amyloid beta by insulysin can contribute to the accumulation of amyloid plaques in the brain.
Related Enzymes[edit | edit source]
Insulysin is related to other metalloproteases such as neprilysin and endothelin-converting enzyme, which also degrade bioactive peptides.
See Also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD