Biology:Proteasome endopeptidase complex
From HandWiki
| Proteasome endopeptidase complex | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Proteasome core particle, di-heptamer, Archaea | |||||||||
| Identifiers | |||||||||
| EC number | 3.4.25.1 | ||||||||
| CAS number | 140879-24-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Proteasome endopeptidase complex (EC 3.4.25.1, ingensin, macropain, multicatalytic endopeptidase complex, prosome, multicatalytic proteinase (complex), MCP, proteasome, large multicatalytic protease, proteasome organelle, alkaline protease, 26S protease, tricorn proteinase, tricorn protease) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Cleavage of peptide bonds with very broad specificity
This 20-S protein is composed of 28 subunits arranged in four rings of seven.
References
- ↑ "Proteasome from Thermoplasma acidophilum: a threonine protease". Science 268 (5210): 579–82. April 1995. doi:10.1126/science.7725107. PMID 7725107. Bibcode: 1995Sci...268..579S.
- ↑ "Structure and functions of the 20S and 26S proteasomes". Annual Review of Biochemistry 65: 801–47. 1996. doi:10.1146/annurev.bi.65.070196.004101. PMID 8811196.
- ↑ "Structure of 20S proteasome from yeast at 2.4 A resolution". Nature 386 (6624): 463–71. April 1997. doi:10.1038/386463a0. PMID 9087403. Bibcode: 1997Natur.386..463G.
- ↑ "Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants". The Journal of Biological Chemistry 273 (40): 25637–46. October 1998. doi:10.1074/jbc.273.40.25637. PMID 9748229.
External links
- Proteasome+endopeptidase+complex at the US National Library of Medicine Medical Subject Headings (MeSH)
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