Application | Comment | Organism |
---|---|---|
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 (Comment) | Organism |
---|---|
recombinant enolase, expressed in Escherichia coli BL21-DE3-pLysS strain harbouring the recombinant pET28a plasmid | Trypanosoma brucei |
Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
2-fluoro-2-phosphonoacetohydroxamate | competitive inhibitor | Trypanosoma brucei | |
phosphonoacetohydroxamate | retains open tunnel from catalytic site to protein surface, offers possibilities for drug development | Trypanosoma brucei | |
SO42- | induces a complete closure of catalytic site loops | Trypanosoma brucei |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | activity depends on | Trypanosoma brucei |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-phospho-D-glycerate | Trypanosoma brucei | - |
phosphoenolpyruvate + H2O | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Trypanosoma brucei | Q9NDH8 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant protein | Trypanosoma brucei |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
activity assay of recombinant protein | Trypanosoma brucei |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-phospho-D-glycerate | - |
Trypanosoma brucei | phosphoenolpyruvate + H2O | - |
r | |
2-phospho-D-glycerate | structural analysis | Trypanosoma brucei | phosphoenolpyruvate + H2O | - |
r |
Synonyms | Comment | Organism |
---|---|---|
enolase | - |
Trypanosoma brucei |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
activity assay at | Trypanosoma brucei |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
activity assay at | Trypanosoma brucei |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0014 | - |
2-fluoro-2-phosphonoacetohydroxamate | at pH 7.2, binds in the same way as phosphoenolpyruvate and phosphonoacetohydroxamate | Trypanosoma brucei | |
0.015 | - |
phosphonoacetohydroxamate | - |
Trypanosoma brucei |