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Proteazomski endopeptidazni kompleks
	Di-heptamer proteazomske jezgarne čestice (Archaea)
Identifikatori
EC broj	3.4.25.1
CAS broj	140879-24-9
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Proteazomski endopeptidazni kompleks (EC 3.4.25.1, ingensin, makropain, multikatalitički endopeptidazni kompleks, prosom, multikatalitička proteinaza (kompleks), MCP, velika multikatalitička proteaza, multikatalitička proteinaza, proteazomska organela, alkalna proteaza, 26S proteaza, trikorn proteinaza, trikorn proteaza) je enzim.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

Razlaganje peptidnih veza sa veoma širokom specifičnošću

Ovaj enzim pripada peptidaznoj familiji T1.

Reference

↑ Seemüller, E., Lupas, A., Stock, D., Löwe, J., Huber, R. and Baumeister, W. (1995). „Proteasome from Thermoplasma acidophilum: a threonine protease”. Science 268: 579-582. 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. 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: 463-471. 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: 25637-25646. PMID 9748229.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Vanjske veze

MeSH Proteasome+endopeptidase+complex

[1] Seemüller, E., Lupas, A., Stock, D., Löwe, J., Huber, R. and Baumeister, W. (1995). „Proteasome from Thermoplasma acidophilum: a threonine protease”. Science 268: 579-582. PMID 7725107.

[2] Coux, O., Tanaka, K. and Goldberg, A.L. (1996). „Structure and functions of the 20S and 26S proteasomes”. Annu. Rev. Biochem. 65: 801-847. PMID 8811196.

[3] 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: 463-471. PMID 9087403.

[4] 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: 25637-25646. PMID 9748229.

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