Eubacterial proteasomes.
Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome of eukaryotes is an ATP-dependent enzyme of about 2 MDa, which acts as the central protease of the ubiquitin-dependent pathway of protein degradation. The core of the 26S complex is formed by the 20S proteasome, an ATP-independent, barrel-shaped protease of about 700 kDa, which has also been detected in archaebacteria and, more recently, in eubacteria. Currently, the distribution of 20S proteasomes in eubacteria appears limited to the actinomycetes, while most other eubacteria contain a related complex of simpler structure.
Lupas
A
A
Max-Planck-Institut für Biochemie, Martinsried, Germany.
Zühl
F
F
Tamura
T
T
Wolf
S
S
Nagy
I
I
De Mot
R
R
Baumeister
W
W
D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology*; D003546:Cysteine Endopeptidases / Q000737:chemistry; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000737:chemistry; D010447:Peptide Hydrolases / Q000737:chemistry*; D046988:Proteasome Endopeptidase Complex; D011487:Protein Conformation
D009097:Multienzyme Complexes; D010447:Peptide Hydrolases; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease