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 | 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 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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Schizosaccharomyces pombe | |
Mg2+ | required | Synechococcus elongatus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Schizosaccharomyces pombe | - |
- |
- |
Synechococcus elongatus | - |
- |
- |
Synechococcus elongatus PCC 7942 | - |
- |
- |
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 | Comment | Organism |
---|---|---|
Hsp90 | - |
Schizosaccharomyces pombe |
Hsp90 | - |
Synechococcus elongatus |
HtpG | - |
Synechococcus elongatus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Schizosaccharomyces pombe |
37 | - |
assay at | Synechococcus elongatus |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Schizosaccharomyces pombe |
8 | - |
assay at | Synechococcus elongatus |
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 |