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Literature summary for 3.6.4.10 extracted from
- A novel C-terminal homologue of Aha1 co-chaperone binds to heat shock protein 90 and stimulates its ATPase activity in Entamoeba histolytica (2014), J. Mol. Biol., 426, 1786-1798.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| EhAha1c | co-chaperone Aha1, i.e. activator of Hsp90 ATPase, lacking a canonical Aha1 N-terminal domain compared to other Aha1 co-chaperones. EhAha1c is capable of binding and stimulating ATPase activity of EhHsp90. The Aha1 protein is characterized by the presence of two domains joined by a small linker, interaction analysis with the enzyme, overview | Entamoeba histolytica |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 pLysS, co-expression with His-tagged EhAha1c | Entamoeba histolytica |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 17-allylamino-17-demethoxygeldanamycin | i.e. tanespimycin, binding kinetics, overview | Entamoeba histolytica |  |
| geldanamycin | a competitive inhibitor of Hsp90 that binds to the ATP-binding pocket in the N-terminal domain of Hsp90 with a higher affinity than ATP, binding kinetics, overview | Entamoeba histolytica | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Entamoeba histolytica | |
| 0.4325 | - |
ATP | recombinant enzyme, pH 7.4, temperature not specified in the publication | Entamoeba histolytica | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Entamoeba histolytica | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Entamoeba histolytica | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 82990 | - |
x * 82990, about, sequence calculation, x * 86000, recombinant His6-tagged enzyme, SDS-PAGE | Entamoeba histolytica |
| 86000 | - |
x * 82990, about, sequence calculation, x * 86000, recombinant His6-tagged enzyme, SDS-PAGE | Entamoeba histolytica |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Entamoeba histolytica | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Entamoeba histolytica HM-1: IMSS | - |
ADP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Entamoeba histolytica | Q5KTW9 | - |
- |
| Entamoeba histolytica HM-1: IMSS | Q5KTW9 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia coli strain BL21 pLysS by nickel affinity chromatograhy | Entamoeba histolytica |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| trophozoite | - |
Entamoeba histolytica | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.412 | - |
purified recombinant enzyme, pH 7.4, temperature not specified in the publication | Entamoeba histolytica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Entamoeba histolytica | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Entamoeba histolytica HM-1: IMSS | ADP + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 82990, about, sequence calculation, x * 86000, recombinant His6-tagged enzyme, SDS-PAGE | Entamoeba histolytica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| heat shock protein 90 | - |
Entamoeba histolytica |
| Hsp90 | - |
Entamoeba histolytica |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00018 | - |
ATP | recombinant enzyme, pH 7.4, temperature not specified in the publication | Entamoeba histolytica | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Entamoeba histolytica |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | inhibition kinetics | Entamoeba histolytica |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Entamoeba histolytica | sequence calculation | - |
4.97 |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.000546 | - |
inhibition of cell growth, pH 7.4, temperature not specified in the publication | Entamoeba histolytica | 17-allylamino-17-demethoxygeldanamycin | |
| 0.0309 | - |
inhibition of the ATPase activity, pH 7.4, temperature not specified in the publication | Entamoeba histolytica | 17-allylamino-17-demethoxygeldanamycin | |
| 0.115 | - |
inhibition of the ATPase activity, in presence of co-chaperone EhAha1c, pH 7.4, temperature not specified in the publication | Entamoeba histolytica | 17-allylamino-17-demethoxygeldanamycin | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | inhibition of Hsp90 by geldanamycin disrupts substrate maturation, leading to derailment of many cellular pathways and, ultimately, cell death | Entamoeba histolytica |
| additional information | distribution of co-chaperones in Entamoeba histolytica, overview | Entamoeba histolytica |
| physiological function | dependence of Entamoeba histolytica on Hsp90 for its growth and survival. Hsp90 plays a critical role in manifestation of infection by virulent human and animal pathogens. Hsp90 function is regulated by various co-chaperones, e.g. by co-chaperone Aha1 (activator of Hsp90 ATPase), EhAha1c, lacking a canonical Aha1 N-terminal domain. These proteins can regulate Hsp90 in multiple ways either by regulating the ATPase activity, by priming it to interact with a certain client group, by assisting in formation of a multichaperone complex, or by aidingin client maturation | Entamoeba histolytica |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.007 | - |
ATP | recombinant enzyme, pH 7.4, temperature not specified in the publication | Entamoeba histolytica | |
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