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Literature summary for 4.1.1.32 extracted from
- A GTP-dependent vertebrate-type phosphoenolpyruvate carboxykinase from Mycobacterium smegmatis (2001), J. Biol. Chem., 276, 16137-16145.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | maximum stimulation at 75 mM | Mycolicibacterium smegmatis |  |
| dithiothreitol | maximum at 10-40 mM, 30% stimulation | Mycolicibacterium smegmatis | |
| reduced glutathione | maximum stimulation at 20 mM | Mycolicibacterium smegmatis | |
| thiol-containing reducing agent | activates | Mycolicibacterium smegmatis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| pck gene, overexpression in Escherichia coli C41(DE3), sequencing | Mycolicibacterium smegmatis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| alpha-ketoglutarate | inhibits oxaloacetate formation, mixed-type inhibition | Mycolicibacterium smegmatis | |
| KCl | 0.5 M, 50% inhibition | Mycolicibacterium smegmatis | |
| Na2SO4 | - |
Mycolicibacterium smegmatis | |
| NaCl | 0.5 M, 50% inhibition | Mycolicibacterium smegmatis | |
| oxalate | potent inhibitor of oxaloacetate formation, mixed-type inhibition | Mycolicibacterium smegmatis | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km-values for several divalent cations, the presence of 2 mM Mg2+ greatly lowers the Km-values for Mn2+, 144fold in the presence of dithiothreitol and 9.4fold in the absence of dithiothreitol, and for Co2+ by 230fold, influence of divalent cations on the Km-value for phosphoenolpyruvate | Mycolicibacterium smegmatis | |
| 0.012 | - |
oxaloacetate | pH 7.2, 37°C | Mycolicibacterium smegmatis | |
| 0.013 | - |
GTP | pH 7.2, 37°C | Mycolicibacterium smegmatis | |
| 0.066 | - |
GDP | pH 7.2, 37°C | Mycolicibacterium smegmatis | |
| 0.1 | - |
phosphoenolpyruvate | pH 7.2, 37°C | Mycolicibacterium smegmatis | |
| 0.29 | - |
IDP | pH 7.2, 37°C | Mycolicibacterium smegmatis | |
| 8.3 | - |
CO2 | pH 7.2, 37°C, bicarbonate | Mycolicibacterium smegmatis | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | recombinant enzyme | Mycolicibacterium smegmatis | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator | Mycolicibacterium smegmatis | |
| Mg2+ | requirement for a divalent cation, poor activator, kinetics, Mg2+ is superior in complexing the nucleotide substrate compared with Mn2+ or Co2+ | Mycolicibacterium smegmatis | |
| Mn2+ | requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator | Mycolicibacterium smegmatis | |
| additional information | not activated by Ca2+, Zn2+, Cu2+ or Ni2+ | Mycolicibacterium smegmatis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 71200 | - |
1 * 72000-74000, SDS-PAGE, 1 * 71200, mass spectrometry | Mycolicibacterium smegmatis |
| 83200 | - |
gel filtration | Mycolicibacterium smegmatis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + oxaloacetate | Mycolicibacterium smegmatis | catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP | GDP + phosphoenolpyruvate + CO2 | - |
r | |
| GTP + oxaloacetate | Mycolicibacterium smegmatis mc(2)155 | catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP | GDP + phosphoenolpyruvate + CO2 | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycolicibacterium smegmatis | Q9AGJ6 | - |
- |
| Mycolicibacterium smegmatis mc(2)155 | Q9AGJ6 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Mycolicibacterium smegmatis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Mycolicibacterium smegmatis |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, purified recombinant enzyme, 100 mM sodium phosphate buffer, pH 7, 100 mM NaCl, 1 month, 24% loss of activity | Mycolicibacterium smegmatis |
| 4°C, purified recombinant His-tagged enzyme, 100 mM sodium phosphate buffer, pH 7, 100 mM NaCl, 2 months, 25% loss of activity | Mycolicibacterium smegmatis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + oxaloacetate | GTP-dependent, enzyme prefers the phosphoenolpyruvate synthesis direction | Mycolicibacterium smegmatis | GDP + phosphoenolpyruvate + CO2 | - |
r | |
| GTP + oxaloacetate | catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP | Mycolicibacterium smegmatis | GDP + phosphoenolpyruvate + CO2 | - |
r | |
| GTP + oxaloacetate | GTP-dependent, enzyme prefers the phosphoenolpyruvate synthesis direction | Mycolicibacterium smegmatis mc(2)155 | GDP + phosphoenolpyruvate + CO2 | - |
r | |
| GTP + oxaloacetate | catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP | Mycolicibacterium smegmatis mc(2)155 | GDP + phosphoenolpyruvate + CO2 | - |
r | |
| ITP + oxaloacetate | - |
Mycolicibacterium smegmatis | IDP + phosphoenolpyruvate + CO2 | - |
r | |
| ITP + oxaloacetate | - |
Mycolicibacterium smegmatis mc(2)155 | IDP + phosphoenolpyruvate + CO2 | - |
r | |
| additional information | ADP is a very poor substrate in the reverse reaction | Mycolicibacterium smegmatis | ? | - |
? | |
| additional information | ADP is a very poor substrate in the reverse reaction | Mycolicibacterium smegmatis mc(2)155 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 72000-74000, SDS-PAGE, 1 * 71200, mass spectrometry | Mycolicibacterium smegmatis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GTP/ITP:oxaloacetate carboxylyase (transphosphorylating) | - |
Mycolicibacterium smegmatis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
at pH 7.2 | Mycolicibacterium smegmatis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 7.4 | at 37°C | Mycolicibacterium smegmatis |
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Release 2023.1 (January 2023)
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