Signal peptide peptidase
Signal Peptide Peptidase (SPP) (pronunciation: /ˈsɪɡnəl ˈpiːptɪdaɪz ˈpɛptɪdeɪz/), is an enzyme that plays a crucial role in the protein maturation process. The term "signal peptide peptidase" is derived from the Latin "signum" meaning "sign", and the Greek "peptos" meaning "cooked, digested", referring to its function in protein processing.
Function
The primary function of the Signal Peptide Peptidase is to cleave the signal peptides from the nascent proteins during their translocation across the endoplasmic reticulum membrane. This process is essential for the correct localization and function of these proteins within the cell.
Structure
Signal Peptide Peptidase is an intramembrane protease, meaning it is embedded within the membrane. It is part of the GxGD-type aspartyl protease family, characterized by a conserved motif in the active site.
Clinical Significance
Alterations in the function of Signal Peptide Peptidase have been linked to several diseases, including Alzheimer's disease and Hepatitis C. In Alzheimer's disease, SPP is involved in the processing of the amyloid precursor protein, a key player in the disease's pathology. In Hepatitis C, the virus's life cycle is dependent on the activity of SPP.
See Also
External links
- Medical encyclopedia article on Signal peptide peptidase
- Wikipedia's article - Signal peptide peptidase
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