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Literature summary for 4.3.2.2 extracted from
- Effect of a new non-cleavable substrate analog on wild-type and serine mutants in the signature sequence of adenylosuccinate lyase of Bacillus subtilis and Homo sapiens (2008), Protein Sci., 17, 1162-1174.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D69N | site-directed mutagenesis, the mutant shows altered binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme | Bacillus subtilis |
| H141Q | site-directed mutagenesis, the mutant shows altered binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme | Bacillus subtilis |
| H68A | site-directed mutagenesis, the mutant shows altered binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme | Bacillus subtilis |
| H89Q | site-directed mutagenesis, the mutant shows altered binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme | Bacillus subtilis |
| H89R | site-directed mutagenesis, the mutant shows altered binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme | Bacillus subtilis |
| S262A | site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme | Bacillus subtilis |
| S262H | site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme | Bacillus subtilis |
| S263A | site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme | Bacillus subtilis |
| S263H | site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme | Bacillus subtilis |
| S289A | site-directed mutagenesis, the mutant shows no activity, and altered molecular weight and binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme | Homo sapiens |
| S289H | site-directed mutagenesis, the mutant shows no activity, and altered molecular weight and binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme | Homo sapiens |
| S290A | site-directed mutagenesis, the mutant shows altered molecular weight and binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme | Homo sapiens |
| S290H | site-directed mutagenesis, the mutant shows no activity, and altered molecular weight and binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate | i.e. APBADP, the non-cleavable substrate analogue acts as a competitive inhibitor with respect to either substrate. ASL binds up to 4 mol of APBADP per mole of enzyme tetramer, the enzyme exhibits negative cooperativity. Binding to enzyme mutants, overview | Bacillus subtilis |  |
| adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate | i.e. APBADP, the non-cleavable substrate analogue acts as a competitive inhibitor with respect to either substrate. ASL binds up to 4 mol of APBADP per mole of enzyme tetramer, the enzyme exhibits positive cooperativity | Homo sapiens | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0003 | - |
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | pH 7.0, 25°C, mutant S290A | Homo sapiens | |
| 0.0016 | - |
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | pH 7.0, 25°C, wild-type enzyme | Homo sapiens | |
| 0.0029 | - |
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | pH 7.0, 25°C, wild-type enzyme | Bacillus subtilis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 191000 | - |
wild-type enzyme, light scattering | Bacillus subtilis |
| 192000 | - |
mutant S263H, light scattering | Bacillus subtilis |
| 196000 | - |
mutant S262A, light scattering | Bacillus subtilis |
| 197000 | - |
mutant S263A, light scattering | Bacillus subtilis |
| 199000 | - |
mutant S262H, light scattering | Bacillus subtilis |
| 221000 | - |
mutant S290H, light scattering | Homo sapiens |
| 227000 | - |
wild-type enzyme and mutant S289H, light scattering | Homo sapiens |
| 234000 | - |
mutant S290A, light scattering | Homo sapiens |
| 237000 | - |
mutant S289A, light scattering | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | Bacillus subtilis | i.e. SAICAR | 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate | i.e. AICAR | ? | |
| 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | Homo sapiens | i.e. SAICAR | 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate | i.e. AICAR | ? | |
| additional information | Bacillus subtilis | adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides | ? | - |
? | |
| additional information | Homo sapiens | adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides | ? | - |
? | |
| succinyladenosine monophosphate | Bacillus subtilis | - |
AMP + fumarate | - |
? | |
| succinyladenosine monophosphate | Homo sapiens | - |
AMP + fumarate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
| Homo sapiens | P30566 | - |
- |
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 | uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism | Bacillus subtilis | |
| (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism | Homo sapiens | |
| N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP | uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism | Bacillus subtilis | |
| N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP | uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism | Homo sapiens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Bacillus subtilis |
| additional information | - |
- |
Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | i.e. SAICAR | Bacillus subtilis | 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate | i.e. AICAR | ? | |
| 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | i.e. SAICAR | Homo sapiens | 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate | i.e. AICAR | ? | |
| additional information | adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides | Bacillus subtilis | ? | - |
? | |
| additional information | adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides | Homo sapiens | ? | - |
? | |
| additional information | residue Ser289 is essential for catalysis | Homo sapiens | ? | - |
? | |
| additional information | residues Ser262 and Ser263 in a flexible loop of the enzyme are essential for catalysis | Bacillus subtilis | ? | - |
? | |
| succinyladenosine monophosphate | - |
Bacillus subtilis | AMP + fumarate | - |
? | |
| succinyladenosine monophosphate | - |
Homo sapiens | AMP + fumarate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ASL | - |
Bacillus subtilis |
| ASL | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Bacillus subtilis |
| 25 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Bacillus subtilis |
| 7 | - |
assay at | Homo sapiens |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.16 | - |
adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate | inhibition kinetics, overview | Bacillus subtilis | |
| 0.21 | - |
adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate | inhibition kinetics, overview | Homo sapiens | |
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