Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli, His-tagged recombinant protein | Plasmodium falciparum |
Protein Variants | Comment | Organism |
---|---|---|
E414L | replacement of an interface glutamate residue with a leucine does not result into dimer dissociation | Plasmodium falciparum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
KBr | monomeric form | Plasmodium falciparum | |
KCl | monomeric form | Plasmodium falciparum | |
NaCl | inhibits dimeric and monomeric forms of the enzyme, inhibition stronger for the monomeric form | Plasmodium falciparum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | disruption of subunit-subunit interactions declines enzyme activity 3fold | Plasmodium falciparum | |
0.07 | - |
phosphoenolpyruvate | acitivity for monomers | Plasmodium falciparum | |
0.28 | - |
phosphoenolpyruvate | activity for dimeric form | Plasmodium falciparum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
KBr | dimeric form 10-20% activated, monomeric form strongly inhibited | Plasmodium falciparum | |
KCl | dimeric form 10-20% activated, monomeric form strongly inhibited | Plasmodium falciparum | |
Mg2+ | protects enolases of yeast and of rabbit muscle but not of Plasmodium falciparum from dissociation in presence of imidazol | Plasmodium falciparum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-phospho-D-glycerate | Plasmodium falciparum | - |
phosphoenolpyruvate + H2O | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | Q27727 | - |
- |
Purification (Comment) | Organism |
---|---|
gel-filtration | Plasmodium falciparum |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
kinetic properties of monomeric and dimeric forms of recombinant enolase compared, enzyme activity measured spectrophotometrically by monitoring formation of 2-phospho-D-glycerate, dimeric structure not essential for catalysis, monomeric form indicates a 3fold lower activity | Plasmodium falciparum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-phospho-D-glycerate | - |
Plasmodium falciparum | phosphoenolpyruvate + H2O | - |
r | |
2-phospho-D-glycerate | kinetic and structural properties of monomeric and dimeric forms of recombinant enolase of Plasmodium falciparum compared | Plasmodium falciparum | phosphoenolpyruvate + H2O | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | dissociation studies of homodimeric enolases into their active monomeric forms, analysis of intersubunit interactions and influence on catalytic and structural stability, properties of monomeric enolase determined | Plasmodium falciparum |
Synonyms | Comment | Organism |
---|---|---|
enolase | - |
Plasmodium falciparum |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
thermal stability different in monomeric and dimeric forms, the dimeric form is stable at 37°C and shows 20-25% inactivation at 50°C, the monomeric form is to 80% inactivated at 37°C after 2h and completely inactivated at 50°C | Plasmodium falciparum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
pH-induced dissociation of enolases, half-dissociation point | Plasmodium falciparum |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5 | 5.5 | pH-dependent dissociation reveals that protonation of groups at the intersubunit interface is responsible for dissociation | Plasmodium falciparum |