From Wikipedia, the free encyclopedia
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
-
^ 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.
-
^ 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.
-
^ 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.
-
^ 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
|
---|
A (alpha subunits) | |
---|
B (beta subunits) | |
---|
C (ATPases) | |
---|
D (non-ATPases) | |
---|
E (activator subunits) | |
---|
F (inhibitor subunit) | |
---|
|
---|
Activity | |
---|
Regulation | |
---|
Classification | |
---|
Kinetics | |
---|
Types | |
---|