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Literature summary extracted from

  • Duarte, D.P.; Ferreira, E.R.; Lima, F.M.; Batista, F.; De Groote, M.; Horjales, E.; Miletti, L.C.; Bahia, D.
    Molecular characterization of Trypanosoma evansi mevalonate kinase (TeMVK) (2018), Front. Cell. Infect. Microbiol., 8, 223 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.36 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

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.36 glycosome
-
 Trypanosoma evansi 20015
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.36 Mg2+ required Trypanosoma evansi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.36 ATP + (R)-mevalonate Trypanosoma evansi
-
 ADP + (R)-5-phosphomevalonate
-
 ?
2.7.1.36 ATP + (R)-mevalonate Trypanosoma evansi 29-19
-
 ADP + (R)-5-phosphomevalonate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.36 Trypanosoma evansi
-
-
-
2.7.1.36 Trypanosoma evansi 29-19
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.36 recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Trypanosoma evansi

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.36 trypanosomoid form
-
 Trypanosoma evansi
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.36 11
-
 purified recombinant enzyme, pH 9.0, 37°C Trypanosoma evansi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.36 ATP + (R)-mevalonate
-
 Trypanosoma evansi ADP + (R)-5-phosphomevalonate
-
 ?
2.7.1.36 ATP + (R)-mevalonate
-
 Trypanosoma evansi 29-19 ADP + (R)-5-phosphomevalonate
-
 ?
2.7.1.36 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 ?
-
-
2.7.1.36 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

EC Number Subunits Comment Organism
2.7.1.36 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
2.7.1.36 tetramer 4 * 35540, about, sequence calculation Trypanosoma evansi

Synonyms

EC Number Synonyms Comment Organism
2.7.1.36 MVK
-
 Trypanosoma evansi
2.7.1.36 TeMVK
-
 Trypanosoma evansi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.36 37
-
 assay at Trypanosoma evansi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.36 9
-
 assay at Trypanosoma evansi

General Information

EC Number General Information Comment Organism
2.7.1.36 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
2.7.1.36 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
2.7.1.36 physiological function mevalonate kinase (MVK) converts mevalonic acid to 5-phosphomevalonic acid Trypanosoma evansi