Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.6.1.5 extracted from

  • de la Pena, A.H.; Goodall, E.A.; Gates, S.N.; Lander, G.C.; Martin, A.
    Substrate-engaged 26S proteasome structures reveal mechanisms for ATP-hydrolysis-driven translocation (2018), Science, 362, eaav0725 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.5

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + polypeptide Homo sapiens
-
 ADP + phosphate + unfolded polypeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + polypeptide
-
 Homo sapiens ADP + phosphate + unfolded polypeptide
-
 ?

Subunits

Subunits Comment Organism
heterohexamer single particle cryoelectron microscopy Homo sapiens

Synonyms

Synonyms Comment Organism
26S proteasome
-
 Homo sapiens
AAA+ ATPase
-
 Homo sapiens

General Information

General Information Comment Organism
metabolism the ATPase motor of the 26S proteasome unfolds and translocates targeted protein substrates into the open gate of a proteolytic core while a proteasomal deubiquitinase concomitantly removes substrate-attached ubiquitin chains Homo sapiens