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Literature summary for 4.3.2.2 extracted from
- Elucidation of the substrate specificity, kinetic and catalytic mechanism of adenylosuccinate lyase from Plasmodium falciparum (2008), Biochim. Biophys. Acta, 1794, 642-654.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha | Plasmodium falciparum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S298A | site-directed mutagenesis, the mutation does not lead to gross changes in the structural properties of ASL, but the specific activity of S298A mutant is 1000fold lower than that of the wild enzyme, the specific activity remains unchanged upon variation of pH | Plasmodium falciparum |
| S298C | site-directed mutagenesis, the mutation does not lead to gross changes in the structural properties of ASL, but the activity of the S298C mutant is completely lost | Plasmodium falciparum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 5-aminoimidazole-4-carboxamide ribonucleoside | 50% inhibition at 0.167 mM | Plasmodium falciparum |  |
| AMP | product inhibition competitive versus succinyladenosine monophosphate | Plasmodium falciparum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | thermodynamics and kinetics, initial velocity and transient kinetics of succinyladenosine monophosphate cleavage, overview | Plasmodium falciparum | |
| 0.032 | - |
succinyladenosine monophosphate | pH 7.4, 25°C | Plasmodium falciparum | |
| 0.034 | - |
AMP | pH 7.4, 25°C | Plasmodium falciparum | |
| 0.76 | - |
fumarate | pH 7.4, 25°C | Plasmodium falciparum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 55000 | - |
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry | Plasmodium falciparum |
| 56235 | - |
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry | Plasmodium falciparum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | Plasmodium falciparum | first step common to both de novo and the salvage pathways in purine biosynthesis | 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate | - |
? | |
| additional information | Plasmodium falciparum | adenylosuccinate lyase is the only enzyme in the purine biosynthetic pathway that catalyzes two distinct, but chemically similar reactions | ? | - |
? | |
| succinyladenosine monophosphate | Plasmodium falciparum | second step common to both de novo and the salvage pathways in purine biosynthesis | AMP + fumarate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Plasmodium falciparum | O15918 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | kinetic and catalytic uni-bi rapid equilibrium ordered mechanism, key role for the conserved Ser298 in catalysis and pivotal role of the substrate in the activation of the catalytic base, detailed overview | Plasmodium falciparum | |
| N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP | kinetic and catalytic mechanism, the enzyme follows a rapid equilibrium ordered bi-uni mechanism in the reverse direction in which AMP binds first to the enzyme followed by fumarate, key role for the conserved Ser298 in catalysis and pivotal role of the substrate in the activation of the catalytic base, detailed overview | Plasmodium falciparum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | first step common to both de novo and the salvage pathways in purine biosynthesis | Plasmodium falciparum | 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate | - |
? | |
| 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | i.e. SAICAR, SAICAR synthesis in vitro | Plasmodium falciparum | 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate | i.e. AICAR | r | |
| additional information | adenylosuccinate lyase is the only enzyme in the purine biosynthetic pathway that catalyzes two distinct, but chemically similar reactions | Plasmodium falciparum | ? | - |
? | |
| succinyladenosine monophosphate | - |
Plasmodium falciparum | AMP + fumarate | - |
? | |
| succinyladenosine monophosphate | second step common to both de novo and the salvage pathways in purine biosynthesis | Plasmodium falciparum | AMP + fumarate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry | Plasmodium falciparum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ASL | - |
Plasmodium falciparum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Plasmodium falciparum |
| 37 | - |
reverse reaction SAICAR synthesis | Plasmodium falciparum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.9 | - |
AMP | pH 7.4, 25°C | Plasmodium falciparum | |
| 2.9 | - |
fumarate | pH 7.4, 25°C | Plasmodium falciparum | |
| 7.5 | - |
succinyladenosine monophosphate | pH 7.4, 25°C | Plasmodium falciparum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Plasmodium falciparum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5.8 | 9 | - |
Plasmodium falciparum |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.093 | - |
AMP | pH 7.4, 25°C | Plasmodium falciparum | |
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