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Literature summary for 4.3.2.2 extracted from
- Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism (2007), J. Mol. Biol., 370, 541-554.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| subcloned from the pUC118 into the pET28a vector for expression in Escherichia coli B834DE3 cells | Escherichia coli |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| the crystal structures of wild-type ADL, and mutant-substrate, H171A-ADS, and -product, H171N-AMP-FUM, complexes are determined to 2.0, 1.85, and 2.0 A resolution, respectively | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H171A | mutant to map out the residues involved in adenylosuccinate binding, and to identify the putative catalytic groups | Escherichia coli |
| H171N | mutant to map out the residues involved in adenylosuccinate binding, and to identify the putative catalytic groups | Escherichia coli |
| S295A | mutant to probe the role of S295 in the catalytic mechanism | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate | Escherichia coli | - |
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
? |  |
| N6-(1,2-dicarboxyethyl)AMP | Escherichia coli | - |
fumarate + AMP | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0AB89 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using a Ni-NTA column | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.004 | - |
mutant S295A, pH 7.0 | Escherichia coli |
| 0.008 | - |
mutant H171N, pH 7.0 | Escherichia coli |
| 0.009 | - |
mutant H171A, pH 7.0 | Escherichia coli |
| 0.031 | - |
mutant H171A, pH 8.5 | Escherichia coli |
| 0.04 | - |
mutant H171N, pH 8.5 | Escherichia coli |
| 4.65 | - |
wild-type protein, pH 7.0 | Escherichia coli |
| 16.47 | - |
wild-type protein, pH 8.5 | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate | - |
Escherichia coli | fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
? | |
| 5-aminoimidazole-(N-succinylocarboxamide) ribotide | - |
Escherichia coli | 5-aminoimidazole-4-carboxamide ribotide + fumarate | - |
? | |
| adenylosuccinate | - |
Escherichia coli | AMP + fumarate | - |
? | |
| N6-(1,2-dicarboxyethyl)AMP | - |
Escherichia coli | fumarate + AMP | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | - |
Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| adenylosuccinate lyase | - |
Escherichia coli |
| ADL | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
activity assay | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
activity assay | Escherichia coli |
| 8.5 | - |
activity assay | Escherichia coli |
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