endopeptidase complex
Definition
Target type: cellularcomponent
A protein complex which is capable of endopeptidase activity. [GO_REF:0000088, GOC:bhm, GOC:TermGenie, PMID:1689240]
Endopeptidase complexes are multi-protein assemblies that play a critical role in the hydrolysis of peptide bonds within proteins. They are essential for various cellular processes, including protein degradation, signal transduction, and the processing of bioactive peptides. The cellular component of an endopeptidase complex can vary significantly depending on the specific enzyme and its function. However, some common features include:
- **Membrane-associated complexes:** Many endopeptidases are associated with cellular membranes, particularly the plasma membrane and intracellular organelles. These complexes may contain transmembrane proteins, lipid anchors, or other proteins that interact with membrane components.
- **Cytoplasmic complexes:** Some endopeptidases function in the cytoplasm and may form complexes with other cytoplasmic proteins. These complexes can be involved in protein degradation pathways, such as the ubiquitin-proteasome system.
- **Lysosomal complexes:** Lysosomes are cellular organelles responsible for the degradation of cellular debris and macromolecules. Some endopeptidases, such as cathepsins, are found in lysosomes and form complexes with other lysosomal proteins.
- **Extracellular complexes:** Certain endopeptidases are secreted from cells and function extracellularly. These complexes may contain specific protein domains that facilitate their secretion and interaction with extracellular substrates.
- **Scaffolding proteins:** Endopeptidase complexes often contain scaffolding proteins that provide structural support and regulate the assembly and activity of the complex. These proteins may interact with multiple components of the complex and facilitate their localization within the cell.
- **Regulatory proteins:** The activity of endopeptidase complexes can be regulated by various proteins, including inhibitors, activators, and chaperones. These regulatory proteins may bind to the complex and modulate its activity in response to cellular signals.
- **Substrate specificity:** Endopeptidases exhibit substrate specificity, meaning they preferentially hydrolyze peptide bonds within specific amino acid sequences. The cellular component of an endopeptidase complex may influence its substrate specificity by providing a specific environment or interacting with specific substrates.
In summary, the cellular component of an endopeptidase complex is highly diverse and depends on the specific enzyme and its cellular function. The complexes can be membrane-associated, cytoplasmic, lysosomal, or extracellular, and they often contain scaffolding proteins, regulatory proteins, and other components that influence their activity and substrate specificity.'
"
Proteins (1)
| Protein | Definition | Taxonomy |
|---|---|---|
| Caspase-2 | A caspase-2 that is encoded in the genome of human. [PRO:WCB, UniProtKB:P42575] | Homo sapiens (human) |
Compounds (10)
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| spermine | polyazaalkane; tetramine | antioxidant; fundamental metabolite; immunosuppressive agent | |
| isoquinoline-1,3,4-trione | isoquinoline-1,3,4-trione: structure in first source | ||
| n-methylisatin | N-methylisatin: structure given in first source | ||
| cetylpyridinium chloride anhydrous | cetylpyridinium chloride : A pyridinium salt that has N-hexadecylpyridinium as the cation and chloride as the anion. It has antiseptic properties and is used in solutions or lozenges for the treatment of minor infections of the mouth and throat. tserigel: according to first source contains polyvinylbutyral & cetylpyridinium chloride; UD only lists cetylpyridinium chloride as constituent | chloride salt; organic chloride salt | antiseptic drug; surfactant |
| acetyl-aspartyl-glutamyl-valyl-aspartal | Ac-Asp-Glu-Val-Asp-H : A tetrapeptide consisting of two L-aspartic acid residues, an L-glutamyl residue and an L-valine residue with an acetyl group at the N-terminal and with the C-terminal carboxy group reduced to an aldehyde. It is an inhibitor of caspase-3/7. acetyl-aspartyl-glutamyl-valyl-aspartal: a capase inhibitor | tetrapeptide | protease inhibitor |
| 5-Nitroisatin | indoles | anticoronaviral agent | |
| benzyloxycarbonyl-phe-ala-fluormethylketone | cathepsin B inhibitor : A cysteine protease inhibitor which inhibits cathepsin B (EC 3.4.22.1). | ||
| PF-00835231 | PF-00835231 : A primary alcohol resulting from the cleavage of the phosphate group of the prodrug PF-07304814. It is an inhibitor of SARS-CoV-1 and -2 main protease (3CLpro) and exhibits potent in vitro antiviral activity. | aromatic ether; indolecarboxamide; L-leucine derivative; primary alcohol; pyrrolidin-2-ones; secondary carboxamide | anticoronaviral agent; drug metabolite; EC 3.4.22.69 (SARS coronavirus main proteinase) inhibitor |
| grassystatin a | grassystatin A: isolated from a cyanobacterium, identified as Lyngbya cf.; structure in first source | ||
| MK-8353 | MK-8353 : A member of the class of indazoles that is 1H-indazole substituted by a 6-(propan-2-yloxy)pyridin-3-yl group at position 3 and by a {[(3S)-3-(methylsulfanyl)-1-(2-{4-[4-(1-methyl-1H-1,2,4-triazol-3-yl)phenyl]-3,6-dihydropyridin-1(2H)-yl}-2-oxoethyl)pyrrolidin-3-yl]carbonyl}amino group at position 5. It is a potent and selective inhibitor of ERK1 and ERK2 in vitro (IC50 values of 23.0 nM and 8.8 nM, respectively). The drug is being developed by Merck Sharp & Dohme and is currently in clinical development for the treatment of advanced/metastatic solid tumors. MK-8353: ERK inhibitor used in oncology | aromatic ether; dihydropyridine; indazoles; methyl sulfide; N-alkylpyrrolidine; pyridines; pyrrolidinecarboxamide; secondary carboxamide; tertiary carboxamide; triazoles | antineoplastic agent; apoptosis inducer; EC 2.7.11.24 (mitogen-activated protein kinase) inhibitor |