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Literature summary for 4.3.2.2 extracted from
- Structural and kinetic studies on adenylosuccinate lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzyme (2014), FEBS J., 281, 1642-1658.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| phylogenetic analysis | Mycobacterium tuberculosis |
| phylogenetic analysis | Mycolicibacterium smegmatis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified enzyme, X-ray diffraction structure determination and analysis at 2.16 A resolution | Mycolicibacterium smegmatis |
| purified enzyme, X-ray diffraction structure determination is not possible | Mycobacterium tuberculosis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Mycobacterium tuberculosis | |
| additional information | - |
additional information | Michaelis-Menten kinetics | Mycolicibacterium smegmatis | |
| 0.0437 | - |
succinyladenosine monophosphate | pH 7.6, 37°C | Mycolicibacterium smegmatis |  |
| 0.2042 | - |
succinyladenosine monophosphate | pH 7.6, 37°C | Mycobacterium tuberculosis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-aminoimidazole-(N-succinylocarboxamide) ribotide | Mycobacterium tuberculosis | - |
5-aminoimidazole-4-carboxamide ribotide + fumarate | - |
? | |
| 5-aminoimidazole-(N-succinylocarboxamide) ribotide | Mycolicibacterium smegmatis | - |
5-aminoimidazole-4-carboxamide ribotide + fumarate | - |
? | |
| additional information | Mycobacterium tuberculosis | the activity of the Mycobacterium tuberculosis enzyme is particularly low | ? | - |
? | |
| succinyladenosine monophosphate | Mycobacterium tuberculosis | - |
AMP + fumarate | - |
r | |
| succinyladenosine monophosphate | Mycolicibacterium smegmatis | - |
AMP + fumarate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | - |
- |
- |
| Mycolicibacterium smegmatis | A0R4I6 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-aminoimidazole-(N-succinylocarboxamide) ribotide | - |
Mycobacterium tuberculosis | 5-aminoimidazole-4-carboxamide ribotide + fumarate | - |
? | |
| 5-aminoimidazole-(N-succinylocarboxamide) ribotide | - |
Mycolicibacterium smegmatis | 5-aminoimidazole-4-carboxamide ribotide + fumarate | - |
? | |
| additional information | the activity of the Mycobacterium tuberculosis enzyme is particularly low | Mycobacterium tuberculosis | ? | - |
? | |
| succinyladenosine monophosphate | - |
Mycobacterium tuberculosis | AMP + fumarate | - |
r | |
| succinyladenosine monophosphate | - |
Mycolicibacterium smegmatis | AMP + fumarate | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | the enzyme forms a tight tetramer with three independent stable interfaces, protomer flexibility and partial disorder. The C3 loop is mostly disordered in subunits B and C, the Mycobacterium smegmatis enzyme is the first reported unliganded enzyme structure in which the C3 loop is ordered at least partially | Mycolicibacterium smegmatis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ASL | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Mycobacterium tuberculosis |
| 37 | - |
assay at | Mycolicibacterium smegmatis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.1 | - |
succinyladenosine monophosphate | pH 7.6, 37°C | Mycobacterium tuberculosis | |
| 0.7 | - |
succinyladenosine monophosphate | pH 7.6, 37°C | Mycolicibacterium smegmatis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
- |
Mycobacterium tuberculosis |
| 8 | - |
- |
Mycolicibacterium smegmatis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme structurally resembles the enzymes of the aspartase/fumarase superfamily, conserved flexible C3 loop, phylogenetic analysis | Mycobacterium tuberculosis |
| evolution | the enzyme structure adheres to the fold of the enzymes of the aspartase/fumarase superfamily, conserved flexible C3 loop, phylogenetic analysis | Mycolicibacterium smegmatis |
| additional information | homology modeling of the enzyme structure using the Mycobacterium smegmatis enzyme structure as a template, comparison to the human enzyme structure and other enzymes, structure-function relationship analysis based on the Mycobacterium smegmatis enzyme structure, active site residues, overview | Mycobacterium tuberculosis |
| additional information | structure-function relationship analysis, active site residues, overview | Mycolicibacterium smegmatis |
| physiological function | a housekeeping enzyme | Mycobacterium tuberculosis |
| physiological function | a housekeeping enzyme | Mycolicibacterium smegmatis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.5 | - |
succinyladenosine monophosphate | pH 7.6, 37°C | Mycobacterium tuberculosis | |
| 16.02 | - |
succinyladenosine monophosphate | pH 7.6, 37°C | Mycolicibacterium smegmatis | |
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