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Literature summary for 2.7.1.36 extracted from
- Molecular characterization of Trypanosoma evansi mevalonate kinase (TeMVK) (2018), Front. Cell. Infect. Microbiol., 8, 223 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Trypanosoma evansi |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| glycosome | - |
Trypanosoma evansi | 20015 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Trypanosoma evansi |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + (R)-mevalonate | Trypanosoma evansi | - |
ADP + (R)-5-phosphomevalonate | - |
? | |
| ATP + (R)-mevalonate | Trypanosoma evansi 29-19 | - |
ADP + (R)-5-phosphomevalonate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trypanosoma evansi | - |
- |
- |
| Trypanosoma evansi 29-19 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Trypanosoma evansi |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| trypanosomoid form | - |
Trypanosoma evansi | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 11 | - |
purified recombinant enzyme, pH 9.0, 37°C | Trypanosoma evansi |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + (R)-mevalonate | - |
Trypanosoma evansi | ADP + (R)-5-phosphomevalonate | - |
? | |
| ATP + (R)-mevalonate | - |
Trypanosoma evansi 29-19 | ADP + (R)-5-phosphomevalonate | - |
? | |
| additional information | a coupled assay method is performed using lactic dehydrogenase and pyruvate kinase. Specific activity of the three different oligomeric states of purified TeMVK is evaluated using a fluorescence-based assay. TeMVK is highly active only in its tetrameric form | Trypanosoma evansi | ? | - |
- |
|
| additional information | a coupled assay method is performed using lactic dehydrogenase and pyruvate kinase. Specific activity of the three different oligomeric states of purified TeMVK is evaluated using a fluorescence-based assay. TeMVK is highly active only in its tetrameric form | Trypanosoma evansi 29-19 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | TeMVK is highly active only in its tetrameric form. The secondary structure prediction for TeMVK suggested an arrangement with the N-terminal domain (residues 1-179) organized as seven beta-sheet strands and four alpha-helices, and the C-terminal domain (residues 180-329) organized as five beta-sheet strands and five alpha-helices | Trypanosoma evansi |
| tetramer | 4 * 35540, about, sequence calculation | Trypanosoma evansi |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MVK | - |
Trypanosoma evansi |
| TeMVK | - |
Trypanosoma evansi |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Trypanosoma evansi |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
assay at | Trypanosoma evansi |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the mevalonate pathway is an essential part of isoprenoid biosynthesis leading to production of a diverse class of over 30000 biomolecules including cholesterol, heme, and all steroid hormones. In trypanosomatids, the mevalonate pathway also generates dolichols, which play an essential role in construction of glycosylphosphatidylinositol (GPI) molecules that anchor variable surface proteins (VSGs) to the plasma membrane. Isoprenoid biosynthesis involves one of the most highly regulated enzymes in nature, 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR), which catalyzes the conversion of HMG-CoA to mevalonic acid. The enzyme mevalonate kinase (MVK) subsequently converts mevalonic acid to 5-phosphomevalonic acid. Presence of mevalonate pathway enzymes in vivo in Trypanosoma evansi during the course of infection | Trypanosoma evansi |
| additional information | TeMVK structure homology modeling, overview. The TeMVK displays a catalytic pocket disposed between the N- and C-terminal domains and formed by the three highly conserved motifs, molecular dynamic simulation demonstrates a stable protein conformation | Trypanosoma evansi |
| physiological function | mevalonate kinase (MVK) converts mevalonic acid to 5-phosphomevalonic acid | Trypanosoma evansi |
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