The multicatalytic proteinase (prosome, proteasome): comparison of the eukaryotic and archaebacterial enzyme.
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.
Dahlmann
B
B
Diabetes Forschungsinstitut, Düsseldorf, F.R.G.
Kopp
F
F
Kuehn
L
L
Hegerl
R
R
Pfeifer
G
G
Baumeister
W
W
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology; D009842:Oligopeptides / Q000737:chemistry; D046988:Proteasome Endopeptidase Complex; D011487:Protein Conformation; D051381:Rats; D013045:Species Specificity; D013379:Substrate Specificity; D013822:Thermoplasma / Q000201:enzymology*
D009097:Multienzyme Complexes; D009842:Oligopeptides; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex