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Literature summary extracted from
- Structural flexibility in Trypanosoma brucei enolase revealed by X-ray crystallography and molecular dynamics (2007), FEBS J., 274, 5077-5089.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 4.2.1.11 | drug development | structure and molecular dynamics applied to design irreversible species-specific inhibitors, parasite-specific lysine residue closely to catalytic site identified | Trypanosoma brucei |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.1.11 | recombinant enolase, expressed in Escherichia coli BL21-DE3-pLysS strain harbouring the recombinant pET28a plasmid | Trypanosoma brucei |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.2.1.11 | hanging drop method, six novel crystal structures with various ligation states and conformations identified, high structural diversity of loops near the catalytic site determined, novel metal-binding site within the catalytic site identified | Trypanosoma brucei |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.11 | 2-fluoro-2-phosphonoacetohydroxamate | competitive inhibitor | Trypanosoma brucei |  |
| 4.2.1.11 | phosphonoacetohydroxamate | retains open tunnel from catalytic site to protein surface, offers possibilities for drug development | Trypanosoma brucei | |
| 4.2.1.11 | SO42- | induces a complete closure of catalytic site loops | Trypanosoma brucei | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.11 | Mg2+ | activity depends on | Trypanosoma brucei | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.11 | 2-phospho-D-glycerate | Trypanosoma brucei | - |
phosphoenolpyruvate + H2O | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.11 | Trypanosoma brucei | Q9NDH8 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.1.11 | recombinant protein | Trypanosoma brucei |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.11 | additional information | - |
activity assay of recombinant protein | Trypanosoma brucei |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.11 | 2-phospho-D-glycerate | - |
Trypanosoma brucei | phosphoenolpyruvate + H2O | - |
r | |
| 4.2.1.11 | 2-phospho-D-glycerate | structural analysis | Trypanosoma brucei | phosphoenolpyruvate + H2O | - |
r | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.11 | enolase | - |
Trypanosoma brucei |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.11 | 25 | - |
activity assay at | Trypanosoma brucei |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.11 | 7.5 | - |
activity assay at | Trypanosoma brucei |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.1.11 | 0.0014 | - |
2-fluoro-2-phosphonoacetohydroxamate | at pH 7.2, binds in the same way as phosphoenolpyruvate and phosphonoacetohydroxamate | Trypanosoma brucei | |
| 4.2.1.11 | 0.015 | - |
phosphonoacetohydroxamate | - |
Trypanosoma brucei | |
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Release 2023.1 (January 2023)
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