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Literature summary for 3.6.4.10 extracted from

  • Yokoyama, Y.; Ohtaki, A.; Jantan, I.; Yohda, M.; Nakamoto, H.
    Goniothalamin enhances the ATPase activity of the molecular chaperone Hsp90 but inhibits its chaperone activity (2015), J. Biochem., 157, 161-168.
    View publication on PubMed
Search for more literature for 3.6.4.10

Activating Compound

Activating Compound Comment Organism Structure
goniothalamin a naturally occurring styryl-lactone, isolated from the air-dried bark of Goniothalamus tapis Miq., that increases both Km and kcat of Hsp90, it binds to the N-terminal domain of Hsp90 activates its ATPase activity, while inhibiting the chaperone function of Hsp90 Schizosaccharomyces pombe
goniothalamin a naturally occurring styryl-lactone, that increases both Km and kcat of Hsp90. Goniothalamin binds to the N-terminal domain of HtpG. Goniothalamin does not influence the interaction of HtpG with a non-native protein or the anti-aggregation activity of HtpG significantly. But it inhibits the activity of HtpG that assists refolding of a non-native protein in cooperation with the Hsp70 chaperone system. Domain competition in presence of goniothalamin, overview. The N-terminal domain inhibits the enhancement of the activity by goniothalamin, whereas HtpG lacking the N-terminal domain, i.e. the middle domain fused to the C-terminal domain, does not affect the enhancement Synechococcus elongatus
tamoxifen a small molecule activator Schizosaccharomyces pombe
tamoxifen a small molecule activator Synechococcus elongatus

Inhibitors

Inhibitors Comment Organism Structure
goniothalamin a naturally occurring styryl-lactone, that increases both Km and kcat of Hsp90, it binds to the N-terminal domain of Hsp90 activates its ATPase activity, while inhibiting the chaperone function of Hsp90 Schizosaccharomyces pombe
goniothalamin a naturally occurring styryl-lactone, isolated from the air-dried bark of Goniothalamus tapis Miq., that increases both Km and kcat of Hsp90. Goniothalamin binds to the N-terminal domain of HtpG. Goniothalamin does not influence the interaction of HtpG with a non-native protein or the anti-aggregation activity of HtpG significantly. But it inhibits the activity of HtpG that assists refolding of a non-native protein in cooperation with the Hsp70 chaperone system. Goniothalamin does not inhibit the refolding assisted by the DnaK chaperone system indicating that goniothalamin exerts an inhibitory effect only on the HtpG-assisted refolding process Synechococcus elongatus
radicicol complete inhibition at 4 nM Synechococcus elongatus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.43
-
 ATP pH 8.0, 37°C in absence of goniothalamin at 0.04 mg/ml Synechococcus elongatus
0.51
-
 ATP pH 8.0, 37°C in absence of goniothalamin at 0.04 mg/ml Schizosaccharomyces pombe
0.66
-
 ATP pH 8.0, 37°C in presence of goniothalamin at 0.04 mg/ml Synechococcus elongatus
0.73
-
 ATP pH 8.0, 37°C in presence of goniothalamin at 0.04 mg/ml Schizosaccharomyces pombe

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Schizosaccharomyces pombe
Mg2+ required Synechococcus elongatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Schizosaccharomyces pombe
-
 ADP + phosphate
-
 ?
ATP + H2O Synechococcus elongatus
-
 ADP + phosphate
-
 ?
ATP + H2O Synechococcus elongatus PCC 7942
-
 ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe
-
-
-
Synechococcus elongatus
-
-
-
Synechococcus elongatus PCC 7942
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Schizosaccharomyces pombe ADP + phosphate
-
 ?
ATP + H2O
-
 Synechococcus elongatus ADP + phosphate
-
 ?
ATP + H2O
-
 Synechococcus elongatus PCC 7942 ADP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
Hsp90
-
 Schizosaccharomyces pombe
Hsp90
-
 Synechococcus elongatus
HtpG
-
 Synechococcus elongatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Schizosaccharomyces pombe
37
-
 assay at Synechococcus elongatus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0195
-
 ATP pH 8.0, 37°C in absence of goniothalamin at 0.04 mg/ml Schizosaccharomyces pombe
0.0253
-
 ATP pH 8.0, 37°C in absence of goniothalamin at 0.04 mg/ml Synechococcus elongatus
0.0408
-
 ATP pH 8.0, 37°C in presence of goniothalamin at 0.04 mg/ml Synechococcus elongatus
0.0438
-
 ATP pH 8.0, 37°C in presence of goniothalamin at 0.04 mg/ml Schizosaccharomyces pombe

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Schizosaccharomyces pombe
8
-
 assay at Synechococcus elongatus

General Information

General Information Comment Organism
physiological function Hsp90 is an ATP-dependent molecular chaperone that is involved in important cellular pathways such as signal transduction pathways. The Hsp90 ATPase activity may facilitate elucidation of the chaperone mechanism of Hsp90 Schizosaccharomyces pombe
physiological function Hsp90 is an ATP-dependent molecular chaperone that is involved in important cellular pathways such as signal transduction pathways. The Hsp90 ATPase activity may facilitate elucidation of the chaperone mechanism of Hsp90 Synechococcus elongatus