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

BRENDA support

Literature summary for 3.6.4.10 extracted from

  • Watanabe, Y.H.; Nakazaki, Y.; Suno, R.; Yoshida, M.
    Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity (2009), Biochem. J., 421, 71-77.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
I403A/L406A/L413A/L420A/L432A/I439A/I446A/L449A residues of hydrophobic interactions Thermus thermophilus
I403A/L406A/L413A/L420A/L432A/I439A/I446A/L449A/I459A/L463A/L470A/V473A/I477A/L492A/L497A/L500A/L507A/L511A residues of hydrophobic interactions Thermus thermophilus
I459A/L463A/L470A/V473A/I477A/L492A/L497A/L500A/L507A/L511A residues of hydrophobic interactions Thermus thermophilus
L406A/L413A/L420A/L432A/I439A/I446A residues of hydrophobic interactions Thermus thermophilus
L406A/L413A/L420A/L432A/I439A/I446A/L463A/L470A/I477A/L492A/L500A/L507A residues of hydrophobic interactions Thermus thermophilus
L413A/L420A/L432A/I439A residues of hydrophobic interactions Thermus thermophilus
L413A/L420A/L432A/I439A/L470A/I477A/L492A/L500A residues of hydrophobic interactions Thermus thermophilus
L463A/L470A/I477A/L492A/L500A/L507A residues of hydrophobic interactions Thermus thermophilus
L470A/I477A/L492A/L500A residues of hydrophobic interactions Thermus thermophilus
additional information mutant proteins show altered ATPase activities Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermus thermophilus

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homohexamer
-
Thermus thermophilus

Synonyms

Synonyms Comment Organism
ClpB chaperone
-
Thermus thermophilus