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Proteasome endopeptidase complex
Proteasome core particle, di-heptamer, Archaea
Identifiers
EC no. 3.4.25.1
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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

  1. ^ Seemüller E, Lupas A, Stock D, Löwe J, Huber R, Baumeister W (April 1995). "Proteasome from Thermoplasma acidophilum: a threonine protease". Science. 268 (5210): 579–82. Bibcode: 1995Sci...268..579S. doi: 10.1126/science.7725107. PMID  7725107.
  2. ^ Coux O, Tanaka K, Goldberg AL (1996). "Structure and functions of the 20S and 26S proteasomes". Annual Review of Biochemistry. 65: 801–47. doi: 10.1146/annurev.bi.65.070196.004101. PMID  8811196.
  3. ^ Groll M, Ditzel L, Löwe J, Stock D, Bochtler M, Bartunik HD, Huber R (April 1997). "Structure of 20S proteasome from yeast at 2.4 A resolution". Nature. 386 (6624): 463–71. Bibcode: 1997Natur.386..463G. doi: 10.1038/386463a0. PMID  9087403. S2CID  4261663.
  4. ^ Dick TP, Nussbaum AK, Deeg M, Heinemeyer W, Groll M, Schirle M, Keilholz W, Stevanović S, Wolf DH, Huber R, Rammensee HG, Schild H (October 1998). "Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants". The Journal of Biological Chemistry. 273 (40): 25637–46. doi: 10.1074/jbc.273.40.25637. PMID  9748229.

External links