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Literature summary for 3.4.25.1 extracted from

  • Kravchuk, O.; Lyupina, Y.; Erokhov, P.; Finoshin, A.; Adameyko, K.; Mishyna, M.; Moiseenko, A.; Sokolova, O.; Orlova, O.; Beljelarskaya, S.; Serebryakova, M.; Indeykina, M.; Bugrova, A.; Kononikhin, A.; Mikhailov, V.
    Characterization of the 20S proteasome of the lepidopteran, Spodoptera frugiperda (2019), Biochim. Biophys. Acta, 1867, 840-853 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
PA200 activator protein Spodoptera frugiperda
PA28 activator protein Spodoptera frugiperda

Crystallization (Commentary)

Crystallization (Comment) Organism
the 20S proteasome core particle forms stable complexes with one or two dimers of assembly chaperones PAC1-PAC2 and activators PA28gamma, PA200 in Spodoptera frugiperda Sf9 cells. Spontaneous detachment of 19S RP from isolated 26S proteasomes leaves core particles at different stages in the gate opening Spodoptera frugiperda

Organism

Organism UniProt Comment Textmining
Spodoptera frugiperda A0A2H1WB52
-
-

Purification (Commentary)

Purification (Comment) Organism
several forms of 20S proteasomes from extracts of Spodoptera frugiperda (Sf9) cells are separated using electrophoresis in a native polyacrylamide gel Spodoptera frugiperda

Subunits

Subunits Comment Organism
More presence of 7 alpha-type and 7 beta-type subunits in the 20S complex Spodoptera frugiperda

Synonyms

Synonyms Comment Organism
SFRICE_003436
-
Spodoptera frugiperda

General Information

General Information Comment Organism
physiological function the 19S regulatory particle in 26S proteasomes performs stepwise substrate unfolding and opens the chamber gate in an ATP-dependent manner. Spontaneous dissociation of the regulatory particle in isolated 26S proteasomes leaves core particles with different gate sizes related presumably to different stages in the gate opening Spodoptera frugiperda