Proteasome endopeptidase complex

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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. and Baumeister, W. (1995). "Proteasome from Thermoplasma acidophilum: a threonine protease". Science 268 (5210): 579–582. doi:10.1126/science.7725107. PMID 7725107.
↑ Coux, O., Tanaka, K. and Goldberg, A.L. (1996). "Structure and functions of the 20S and 26S proteasomes". Annu. Rev. Biochem. 65: 801–847. doi:10.1146/annurev.bi.65.070196.004101. PMID 8811196.
↑ Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H.D. and Huber, R. (1997). "Structure of 20S proteasome from yeast at 2.4Å resolution". Nature 386 (6624): 463–471. doi:10.1038/386463a0. PMID 9087403.
↑ 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. (1998). "Contribution of proteasomal β-subunits to the cleavage of peptide substrates analyzed with yeast mutants". J. Biol. Chem. 273 (40): 25637–25646. 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)

Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase

3.4.11	Aminopeptidase Alanine Arginyl Aspartyl Cystinyl Leucyl Glutamyl Methionyl 1 2 O

3.4.13	Dipeptidase 1 2 3

3.4.14	Dipeptidyl peptidase Cathepsin C Dipeptidyl peptidase-4 Tripeptidyl peptidase Tripeptidyl peptidase I Tripeptidyl peptidase II

3.4.15	Angiotensin-converting enzyme

3.4.16	Serine type carboxypeptidases: Cathepsin A DD-transpeptidase

3.4.17	Metalloexopeptidases Carboxypeptidase A A2 B C E Glutamate II

Other/ungrouped	Metalloexopeptidase

3.4.21-25: Endopeptidase

Other/ungrouped: Amyloid precursor protein secretase

3.4.99: Unknown

Staphylokinase

Proteasome endopeptidase complex subunits (EC 3.4.25.1)

A (alpha subunits)	PSMA1 PSMA2 PSMA3 PSMA4 PSMA5 PSMA6 PSMA7 PSMA8

B (beta subunits)	PSMB1 PSMB2 PSMB3 PSMB4 PSMB5 PSMB6 PSMB7 PSMB8 PSMB9 PSMB10

C (ATPases)	PSMC1 PSMC2 PSMC3 PSMC4 PSMC5 PSMC6

D (non-ATPases)	PSMD1 PSMD2 PSMD3 PSMD4 PSMD5 PSMD6 PSMD7 PSMD8 PSMD9 PSMD10 PSMD11 PSMD12 PSMD13 PSMD14

E (activator subunits)	PSME1 PSME2 PSME3 PSME4

F (inhibitor subunit)	PSMF1

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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