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

BRENDA support

Literature summary for 3.6.4.10 extracted from

  • Yamamoto, S.; Subedi, G.P.; Hanashima, S.; Satoh, T.; Otaka, M.; Wakui, H.; Sawada, K.; Yokota, S.; Yamaguchi, Y.; Kubota, H.; Itoh, H.
    ATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP) (2014), J. Biol. Chem., 289, 9880-9886.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.10

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Sus scrofa 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-
Sus scrofa O02705
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Sus scrofa
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Hsp70
-
 Sus scrofa
Hsp90
-
 Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Sus scrofa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0005
-
 ATP pH 7.4, 37°C Sus scrofa
0.0014
-
 ATP pH 7.4, 37°C Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Sus scrofa

General Information

General Information Comment Organism
physiological function co-chaperones help to maintain cellular homeostasis by modulating the activities of molecular chaperones involved in protein quality control. The HSP70/HSP90-organizing protein (HOP) is a co-chaperone that cooperates with HSP70 and HSP90 in catalysis of protein folding and maturation in the cytosol. HOP has ATP-binding activity comparable to that of HSP70/HSP90, and that HOP slowly hydrolyzes ATP. The ATPase domain of HOP locates in the N-terminal TPR1-DP1-TPR2A segment. HOP changes its conformation in the presence of ATP, its ATPase activity is unaffected by the D186A mutation Sus scrofa