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Literature summary extracted from
- Cysteine is the general base that serves in catalysis by isocitrate lyase and in mechanism-based inhibition by 3-nitropropionate (2014), Biochemistry, 53, 178-187.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.3.1 | expression of the enzyme with a thrombin-cleavable N-terminal His6 tag in Escherichia coli strain BL21(DE3) | Mycobacterium tuberculosis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.3.1 | 3-nitropropionate | a succinate analogue. Inhibition by 3-nitropropionate proceeds through an unusual double slow-onset process featuring formation of a complex with a Ki of 0.0033 mM during the first minute, followed by formation of a final complex with a Ki* of 44 nM over the course of several min to hours | Mycobacterium tuberculosis |  |
| 4.1.3.1 | glyoxylate | - |
Mycobacterium tuberculosis | |
| 4.1.3.1 | Itaconate | a succinate analogue lacking an acidic alpha-proton, the inhhibitor does not display slow-binding behavior | Mycobacterium tuberculosis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.3.1 | additional information | - |
additional information | stopped-flow spectroscopy and steady-state kinetics, solvent kinetic isotope effects, overview. Whereas the D2OV is consistent with partially rate-limiting proton transfer during formation of the hydroxyl group of isocitrate, the large inverse D2O(V/Ksuccinate) indicates that substantially different kinetic parameters exist when the enzyme is saturated with succinate | Mycobacterium tuberculosis | |
| 4.1.3.1 | 0.045 | - |
isocitrate | recombinant detagged enzyme, pH 7.0, 37°C | Mycobacterium tuberculosis | |
| 4.1.3.1 | 0.14 | - |
glyoxylate | recombinant detagged enzyme, pH 7.0, 37°C | Mycobacterium tuberculosis | |
| 4.1.3.1 | 0.412 | - |
succinate | recombinant detagged enzyme, pH 7.0, 37°C | Mycobacterium tuberculosis | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.3.1 | Mg2+ | required | Mycobacterium tuberculosis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.3.1 | isocitrate | Mycobacterium tuberculosis | - |
succinate + glyoxylate | - |
r | |
| 4.1.3.1 | isocitrate | Mycobacterium tuberculosis H37R | - |
succinate + glyoxylate | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.3.1 | Mycobacterium tuberculosis | - |
- |
- |
| 4.1.3.1 | Mycobacterium tuberculosis H37R | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.3.1 | recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nicke affinity chromatography, cleavage of the His-tag by thrombin, and dialysis | Mycobacterium tuberculosis |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.1.3.1 | isocitrate = succinate + glyoxylate | common mechanism for catalysis with succinate: (1) an unfavorable prebinding isomerization of the active site Cys191-His193 pair to the thiolate-imidazolium form, a process that is favored in D2O, and (2) the transfer of a proton from succinate or 3-NP to Cys191 | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.3.1 | isocitrate | - |
Mycobacterium tuberculosis | succinate + glyoxylate | - |
r | |
| 4.1.3.1 | isocitrate | - |
Mycobacterium tuberculosis H37R | succinate + glyoxylate | - |
r | |
| 4.1.3.1 | succinate + glyoxylate | - |
Mycobacterium tuberculosis | isocitrate | - |
r | |
| 4.1.3.1 | succinate + glyoxylate | - |
Mycobacterium tuberculosis H37R | isocitrate | - |
r | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.3.1 | ICL | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.3.1 | 37 | - |
assay at | Mycobacterium tuberculosis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.3.1 | 8.5 | - |
succinate | recombinant detagged enzyme, pH 7.0, 37°C | Mycobacterium tuberculosis | |
| 4.1.3.1 | 12.2 | - |
isocitrate | recombinant detagged enzyme, pH 7.0, 37°C | Mycobacterium tuberculosis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.3.1 | 7 | - |
assay at | Mycobacterium tuberculosis |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.3.1 | additional information | - |
additional information | solvent isotope effects in inhibition by itaconate and 3-nitropropionate, overview | Mycobacterium tuberculosis | |
| 4.1.3.1 | 4.3 | - |
glyoxylate | recombinant detagged enzyme, pH 7.0, 37°C | Mycobacterium tuberculosis | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.1.3.1 | physiological function | the enzyme catalyzes the first committed step in the glyoxylate cycle, it is essential in Mycobacterium tuberculosis for cell survival during chronic infection | Mycobacterium tuberculosis |
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