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

BRENDA support

Literature summary for 3.6.4.10 extracted from

  • Ranaweera, C.B.; Glaza, P.; Yang, T.; Zolkiewski, M.
    Interaction of substrate-mimicking peptides with the AAA+ ATPase ClpB from Escherichia coli (2018), Arch. Biochem. Biophys., 655, 12-17 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
E279Q/E678Q ATP-hydrolysis deficient substrate-trapping variant Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
570000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Escherichia coli
-
ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Escherichia coli ADP + phosphate
-
?

Subunits

Subunits Comment Organism
hexamer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
AAA+ ATPase
-
Escherichia coli
ClpB
-
Escherichia coli

General Information

General Information Comment Organism
metabolism the enzyme ClpB disaggregates and reactivates aggregated proteins in cooperation with the Hsp70/Hsp40 chaperones DnaK, DnaJ, and GrpE. The substrate recognition mechanism of ClpB relies on global surface properties of aggregated proteins Escherichia coli