5-oxoprolyl-peptidase
| 5-oxoprolyl-peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Script error: No such module "InfoboxImage". | |||||||||
| Identifiers | |||||||||
| EC number | 3.4.19.3 | ||||||||
| CAS number | 9025-49-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
5-oxoprolyl-peptidase (EC 3.4.19.3), also known as pyroglutamyl-peptidase, is an enzyme that catalyzes the hydrolysis of the N-terminal pyroglutamyl group from polypeptides. This enzyme is important in the metabolism of peptides and proteins, particularly in the processing of glutathione and other peptides that contain pyroglutamyl residues.
Function[edit | edit source]
5-oxoprolyl-peptidase specifically cleaves the pyroglutamyl (5-oxoproline) residue from the N-terminus of peptides. This reaction is crucial for the degradation and recycling of peptides that have been modified by the addition of a pyroglutamyl group. The enzyme is involved in the regulation of peptide hormones and neuropeptides, as well as in the detoxification of certain compounds.
Structure[edit | edit source]
The enzyme is a member of the peptidase family C15 and is characterized by its ability to recognize and cleave the pyroglutamyl group. The active site of 5-oxoprolyl-peptidase contains a catalytic triad that is essential for its enzymatic activity. The structure of the enzyme allows it to specifically bind to the pyroglutamyl group and facilitate its removal from the peptide chain.
Biological significance[edit | edit source]
5-oxoprolyl-peptidase plays a significant role in the metabolism of glutathione, a tripeptide that is critical for cellular antioxidant defense. By removing the pyroglutamyl group, the enzyme helps maintain the balance of glutathione and other peptides in the cell. Additionally, the enzyme is involved in the processing of peptide hormones and neuropeptides, which are important for various physiological functions.
Clinical relevance[edit | edit source]
Alterations in the activity of 5-oxoprolyl-peptidase have been associated with certain diseases and conditions. For example, deficiencies in this enzyme can lead to the accumulation of pyroglutamyl peptides, which may contribute to oxidative stress and cellular damage. Understanding the role of 5-oxoprolyl-peptidase in health and disease can provide insights into potential therapeutic targets for conditions related to peptide metabolism.
Also see[edit | edit source]
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Contributors: Prab R. Tumpati, MD
