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Literature summary extracted from
- Enzymatic and biological characteristics of enolase in Brucella abortus A19 (2012), Mol. Biol. Rep., 39, 2705-2711.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.1.11 | expression of His-tagged enolase in Escherichia coli strain BL21 | Brucella abortus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.11 | Cr2+ | leads to complete inhibition at 10 mM | Brucella abortus |  |
| 4.2.1.11 | Cu2+ | leads to complete inhibition at 10 mM | Brucella abortus | |
| 4.2.1.11 | Hg2+ | leads to complete inhibition at 10 mM | Brucella abortus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.1.11 | 2 | - |
2-phospho-D-glycerate | pH 8.5, 25°C, recombinant enzyme | Brucella abortus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.11 | Al3+ | can partially substitute for Mg2+ or Zn2+ at 10 mM showing 68.8% of the maximal activity with 10 mM Mg2+ | Brucella abortus | |
| 4.2.1.11 | Mg2+ | activates, optimally at 10 mM | Brucella abortus | |
| 4.2.1.11 | Mn2+ | can partially substitute for Mg2+ or Zn2+ at 10 mM showing 90.4% of the maximal activity with 10 mM Mg2+ | Brucella abortus | |
| 4.2.1.11 | additional information | 57% of maximal activity without metal ion compared to Mg2+ at 10 mM | Brucella abortus | |
| 4.2.1.11 | Ni2+ | can partially substitute for Mg2+ or Zn2+ at 10 mM showing 90.5% of the maximal activity with 10 mM Mg2+ | Brucella abortus | |
| 4.2.1.11 | Zn2+ | activates, optimally at 10 mM, best activating metal ion | Brucella abortus | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.11 | 49000 | - |
x * 49000, recombinant His-tagged enolase, SDS-PAGE | Brucella abortus |
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 | Brucella abortus | - |
phosphoenolpyruvate + H2O | - |
? | |
| 4.2.1.11 | 2-phospho-D-glycerate | Brucella abortus A19 | - |
phosphoenolpyruvate + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.11 | Brucella abortus | Q2YPV0 | strain 2308, 100% sequence identity with strain A19 | - |
| 4.2.1.11 | Brucella abortus A19 | Q2YPV0 | strain 2308, 100% sequence identity with strain A19 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.1.11 | recombinant His-tagged enolase from Escherichia coli strain BL21 by nickel affinity chromatography | Brucella abortus |
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 | 3909 | - |
purifed recombinant enzyme, pH 8.5, 37°C, no metal ion added | Brucella abortus |
| 4.2.1.11 | 9091 | - |
purifed recombinant enzyme, pH 8.5, 37°C, 10 mM Mg2+ | Brucella abortus |
| 4.2.1.11 | 10050 | - |
purifed recombinant enzyme, pH 8.5, 37°C, 10 mM Zn2+ | Brucella abortus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.11 | 2-phospho-D-glycerate | - |
Brucella abortus | phosphoenolpyruvate + H2O | - |
? | |
| 4.2.1.11 | 2-phospho-D-glycerate | - |
Brucella abortus A19 | phosphoenolpyruvate + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.2.1.11 | ? | x * 49000, recombinant His-tagged enolase, SDS-PAGE | Brucella abortus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.11 | enolase | - |
Brucella abortus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.11 | 37 | - |
recombinant enzyme | Brucella abortus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.11 | 25 | 62 | maximally stable at 37°C, the purified recombinant enolase is thermally stable at 25°C, 37°C, 50°C, and 62°C, but is completely inhibited by a preincubation of the enzyme at 75°C after 1 h | Brucella abortus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.11 | 8.5 | - |
recombinant enzyme | Brucella abortus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.11 | 5 | 10 | activity range, recombinant enzyme | Brucella abortus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.1.11 | physiological function | the recombinant enolase exhibits fibronectin-binding ability in immunoblotting assay, suggesting that enolase may play a role in Brucella abortus colonization, persistence, and invasion of host tissue | Brucella abortus |
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