The multicatalytic proteinase (prosome, proteasome): comparison of the 
eukaryotic and archaebacterial enzyme

Dahlmann, B.; Kopp, F.; Kühn, L.; Hegerl, R.; Pfeifer, G.; Baumeister, W.

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The multicatalytic proteinase (prosome, proteasome): comparison of the eukaryotic and archaebacterial enzyme

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Citation

Dahlmann, B., Kopp, F., Kühn, L., Hegerl, R., Pfeifer, G., & Baumeister, W. (1991). The multicatalytic proteinase (prosome, proteasome): comparison of the eukaryotic and archaebacterial enzyme. Biomedica Biochimica Acta., 50(4-6), 465-469.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-744D-F

Abstract

Proteasomes isolated and purified from rat muscle tissue and from the archaebacterium Thermoplasma acidophilum have a very similar size and shape, but the subunit composition is less complex in the archaebacterium as compared to the eukaryotic particle. The archaebacterial enzyme contains a catalytic site with chymotryptic specificity, which is inhibited by serine proteinase inhibitors and clearly differs from the eukaryotic particle which has a minimum of three catalytic sites for peptide bond hydrolysis of a yet undefined mechanism.