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Literature summary for 3.6.4.10 extracted from
- Human mitochondrial Hsp70 (mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization (2015), PLoS ONE, 10, e0117170.
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | Hsp70 proteins are targets for the drug-based treatments for cancers, misfolding diseases, and protein folding disorders | Homo sapiens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), production of folded and soluble recombinant mortalin when co-expressed with the human Hsp70-escort protein 1, but Hsp70 is still likely prone to self-association | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant enzyme, X-ray diffraction structure determination and analysis, small angle X-ray scattering, modeling | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Homo sapiens | |
| 0.19 | - |
ATP | recombinant enzyme, pH 7.5, 37°C | Homo sapiens |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Homo sapiens | 5739 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Homo sapiens | - |
ADP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P38646 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme by nickel affinity chromatography and gel filtration | Homo sapiens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.00086 | - |
purified recombinant enzyme, pH 7.5, 37°C | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Homo sapiens | ADP + phosphate | - |
? | |
| additional information | mortalin interacts with adenosine nucleotides with high affinity | Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 36000-66000, recombinant enzyme, monomeric and monodisperse mortalin, analytical ultracentrifugation and crystal structure analysis, mortalin has an elongated shape in solution, modeling, overview | Homo sapiens |
| More | secondary and tertiary structures of mortalin, mortalin is formed by at least two domains with different stabilities, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GRP75 | - |
Homo sapiens |
| HspA9 | - |
Homo sapiens |
| mitochondrial hsp70 | - |
Homo sapiens |
| mortalin | - |
Homo sapiens |
| mtHSP70 | - |
Homo sapiens |
| PBP74 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0025 | - |
ATP | recombinant enzyme, pH 7.5, 37°C | Homo sapiens | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | a highly conserved molecular chaperone of the Hsp70 family that is primarily found in the mitochondria | Homo sapiens |
| malfunction | in vivo deregulation of mortalin expression and/or function is correlated with agerelated diseases and certain cancers due to its interaction with the p53 protein | Homo sapiens |
| additional information | mortalin is formed by at least two domains, the transition is sensitive to the presence of adenosine nucleotides and the process is dependent on the presence of Mg2+ ions. Thermal-induced unfolding assays of mortalin suggest the presence of an aggregation/association event, which may explain its natural tendency for in vivo aggregation | Homo sapiens |
| physiological function | the enzyme is of considerable importance for mitochondria biogenesis and the correct functioning of the cell machinery. In the mitochondrial matrix, mortalin acts in the importing and folding process of nucleus-encoded proteins, mortalin is the import motor that drives the preprotein import process and helps the folding of these proteins in the mitochondrial matrix. Depending on its localization and its binding partners, mortalin is associated with several functions, overview | Homo sapiens |
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