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Ubiquitin-Proteasome
Ubiquitin-Proteasome Interactive Pathway: Proteasome
 

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Functional Class : proteasome endopeptidase complex

Name proteasome endopeptidase complex
Description multicatalytic endopeptidase complex
URN urn:agi-enz:3.4.25.1
Total Controls 0
Total Nodes 0
Total Members 0
Notes A 20-S protein composed of 28 subunits arranged in four rings of seven. The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. The molecule is barrel-shaped, and the active sites are on the inner surfaces. Terminal apertures restrict access of substrates to the active sites. There is evidence that catalytic subunits are replaced by others under some conditions so as to alter the specificity of proteolysis, perhaps optimizing it for the formation of antigenic peptides. A complex of the 20-S proteasome endopeptidase complex with a 19-S regulatory unit is the 26-S proteasome that degrades ubiquitin-protein conjugates. Type example of peptidase family T1. Formerly EC 3.4.24.5, EC 3.4.22.21 and EC 3.4.99.46
Connectivity 0

Cell Localization Cytoplasm

Alias proteasome endopeptidase complex
ingensin
macropain
multicatalytic endopeptidase complex
prosome
multicatalytic proteinase (complex)
MCP
proteasome
large multicatalytic protease
multicatalytic proteinase
proteasome organelle
alkaline protease
26S protease
tricorn proteinase
tricorn protease

LocusLink ID 24967
16912
5698
24968
50601
16913
5696
29666
19175
5694
29668
26440
5682
29669
19166
5683
29670
19167
5684
29671
26441
5685
29672
26442
103084
5686
29673
26443
5687
29675
26445
27983
100341
100397
5690
29676
26446
5691
220568
58854
19172
5692
85492
19177
5695
94198
19170
98079
106483
5689
19171
5699
8138
29425
19173
5693
29674
26444
5688

EC Number 3.4.25.1

Class Hydrolases
Acting on peptide bonds (peptidases)
Threonine endopeptidases

Genes 5682(PSMA1)
5683(PSMA2)
5684(PSMA3)
5685(PSMA4)
5686(PSMA5)
5687(PSMA6)
5688(PSMA7)
5689(PSMB1)
5690(PSMB2)
5691(PSMB3)
5692(PSMB4)
5693(PSMB5)
5694(PSMB6)
5695(PSMB7)
5696(PSMB8)
5698(PSMB9)
5699(PSMB10)

Disease MIM: 176842 Proteasome (prosome, macropain) subunit, alpha type, 2
MIM: 176843 Proteasome (prosome, macropain) subunit, alpha type, 3
MIM: 176844 Proteasome component 5
MIM: 600306 Proteasome subunit, beta type, 5
MIM: 602017 Proteasome (prosome, macropain) subunit, beta type, 1
MIM: 602175 Proteasome subunit, beta type, 2
MIM: 602176 Proteasome subunit, beta type, 3
MIM: 602177 Proteasome subunit, beta type, 4
MIM: 602854 Proteasome subunit, alpha-type, 1
MIM: 604030 Proteasome subunit, beta-type, 7
MIM: 606607 Proteasome subunit, alpha-type, 7

PDB ID 1J2P
1J2Q
1Q5Q
1Q5R

Reference Seemuller, E., Lupas, A., Stock, D., Lowe, J., Huber, R. and Baumeister, W. Proteasome from Thermoplasma acidophilum: a threonine protease. Science 268 (1995) 579-582. 2 [PMID:8811196] Coux, O., Tanaka, K. and Goldberg, A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65 (1996) 801-847. 3 [PMID:9087403] Groll, M., Ditzel, L., Lowe, J., Stock, D., Bochtler, M., Bartunik, H.D. and Huber, R. Structure of 20S proteasome from yeast at 2.4A resolution. Nature 386 (1997) 463-471. 4 [PMID:9748229] Dick, T.P., Nussbaum, A.K., Deeg, M., Heinemeyer, W., Groll, M., Schirle, M., Keilholz, W., Stevanovic, S., Wolf, D.H., Huber, R., Rammensee, H.G. and Schild, H. Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants. J. Biol. Chem.386 (1998) 25637-25646.

DB Link IUBMB Enzyme Nomenclature: 3.4.25.1
ExPASy - ENZYME nomenclature database: 3.4.25.1
ERGO genome analysis and discovery system: 3.4.25.1
BRENDA, the Enzyme Database: 3.4.25.1
CAS: 140879-24-9

Source KEGG

CAS ID 140879-24-9