The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria.
From the thermoacidophilic archaebacterium, Thermoplasma acidophilum, a proteolytically active particle has been isolated which is almost identical in size and shape with the multicatalytic proteinase (prosome) from rat. This result indicates that prosomes have been developed early in evolution and that they possibly serve functions common to all living cells.
Dahlmann
B
B
Diabetes Forschungsinstitut, Auf'm Hennekamp, Düsseldorf, FRG.
Kopp
F
F
Kuehn
L
L
Niedel
B
B
Pfeifer
G
G
Hegerl
R
R
Baumeister
W
W
D000818:Animals; D001105:Archaea / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology*; D005075:Biological Evolution; D002122:Calcium Chloride / Q000494:pharmacology; D002845:Chromatography; D003546:Cysteine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification* / Q000378:metabolism; D009132:Muscles / Q000201:enzymology; D010446:Peptide Fragments; D046988:Proteasome Endopeptidase Complex; D051381:Rats; D013379:Substrate Specificity
D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D010446:Peptide Fragments; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D002122:Calcium Chloride