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Literature summary for 5.6.1.5 extracted from

  • Peth, A.; Uchiki, T.; Goldberg, A.L.
    ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation (2010), Mol. Cell, 40, 671-681.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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Synonyms

Synonyms Comment Organism
19S ATPase
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Oryctolagus cuniculus

General Information

General Information Comment Organism
physiological function cofactor requirements for conjugate binding and the contributions of individual 19S subunits to this process are defined. The initial high-affinity association depends only on the ubiquitin chain, is stimulated by ATP binding, but is also readily reversible. Then a temperature-dependent step that requires ATP hydrolysis and a loose domain on the ubiquitinated protein leads to tighter binding of the substrate. This step precedes the removal and disassembly of the ubiquitin chain and seems to serve an editing function that distinguishes proteins capable of complete hydrolysis Oryctolagus cuniculus