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Literature summary for 7.2.2.10 extracted from

  • Tupling, A.R.; Gramolini, A.O.; Duhamel, T.A.; Kondo, H.; Asahi, M.; Tsuchiya, S.C.; Borrelli, M.J.; Lepock, J.R.; Otsu, K.; Hori, M.; MacLennan, D.H.; Green, H.J.
    HSP70 binds to the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA1a) and prevents thermal inactivation (2004), J. Biol. Chem., 279, 52382-52389.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
HSP70 chaperone system can bind to enzyme and, depending on the severity of heat stress, protect the enzyme's function by stabilizing the nucleotide binding domain Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
transfection in HEK-293 cells Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
sarcoplasmic reticulum
-
Rattus norvegicus 16529
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
gastrocnemius
-
Rattus norvegicus
-

Synonyms

Synonyms Comment Organism
SERCA1a
-
Rattus norvegicus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
the maximal activity is reduced progressively with increasing temperature and time of incubation Rattus norvegicus