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Literature summary extracted from
- Aspartate ammonia-lyase (1985), Methods Enzymol., 113, 618-627.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.1 | acid anhydride | activates | Escherichia coli |  |
| 4.3.1.1 | alpha-methyl-DL-aspartate | activates | Escherichia coli | |
| 4.3.1.1 | N-hydroxysuccinimide acetate | activates | Escherichia coli | |
| 4.3.1.1 | subtilisin BPN' | activates | Escherichia coli | |
| 4.3.1.1 | Trypsin | enzyme is activated several-fold by limited treatment | Escherichia coli |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.3.1.1 | - |
Pseudomonas fluorescens |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 4.3.1.1 | enzyme is fairly stable in the presence of high concentrations of ammonium sulfate, potassium phosphate, and KCl | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.1 | 5,5'-dithiobis(2-nitrobenzoate) | - |
Escherichia coli | |
| 4.3.1.1 | aspartate beta-semialdehyde | i.e. aspartic beta-semialdehyde.Inactivates as an active-site directed agent | Escherichia coli | |
| 4.3.1.1 | D-Aspartate | competitive | Escherichia coli | |
| 4.3.1.1 | diethyldicarbonate | reactivated by hydroxylamine | Escherichia coli | |
| 4.3.1.1 | EDTA | partial | Escherichia coli | |
| 4.3.1.1 | p-hydroxymercuribenzoate | - |
Escherichia coli | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.1.1 | 2.4 | - |
L-aspartate | in the presence of 3 mM MgCl2, pH 9.0 | Pseudomonas fluorescens | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.1 | Mg2+ | activates at the alkine pH | Escherichia coli | |
| 4.3.1.1 | Mg2+ | activates at the alkine pH | Hafnia alvei | |
| 4.3.1.1 | Mn2+ | - |
Hafnia alvei | |
| 4.3.1.1 | Mn2+ | activates at the alkine pH | Escherichia coli | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.1 | 173000 | - |
sedimentation equilibrium analysis | Pseudomonas fluorescens |
| 4.3.1.1 | 193000 | - |
sedimentation equilibrium analysis | Escherichia coli |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.1.1 | additional information | Escherichia coli | enzyme synthesis is subject to catabolite repression by glucose and is suppressed under aerobic conditions | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.1.1 | Escherichia coli | - |
- |
- |
| 4.3.1.1 | Hafnia alvei | - |
- |
- |
| 4.3.1.1 | Pseudomonas fluorescens | - |
IFO 3081 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.3.1.1 | - |
Escherichia coli |
| 4.3.1.1 | - |
Pseudomonas fluorescens |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.1 | 68.5 | - |
- |
Escherichia coli |
| 4.3.1.1 | 229 | - |
- |
Pseudomonas fluorescens |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 4.3.1.1 | 2-mercaptoethanol and dithiothreitol protect enzyme against inactivation during storage | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.1.1 | fumarate + hydroxylamine | substrates for reverse reaction | Escherichia coli | ? | - |
? | |
| 4.3.1.1 | fumarate + NH4Cl | substrates for reverse reaction | Escherichia coli | ? | - |
? | |
| 4.3.1.1 | L-aspartate | r | Escherichia coli | fumarate + NH3 | - |
? | |
| 4.3.1.1 | L-aspartate | r | Pseudomonas fluorescens | fumarate + NH3 | - |
? | |
| 4.3.1.1 | L-aspartate | r | Hafnia alvei | fumarate + NH3 | - |
? | |
| 4.3.1.1 | L-aspartate | absolutely specific | Escherichia coli | fumarate + NH3 | - |
? | |
| 4.3.1.1 | L-aspartate | natural substrate | Escherichia coli | fumarate + NH3 | - |
? | |
| 4.3.1.1 | L-aspartate | natural substrate | Pseudomonas fluorescens | fumarate + NH3 | - |
? | |
| 4.3.1.1 | L-aspartate | natural substrate | Hafnia alvei | fumarate + NH3 | - |
? | |
| 4.3.1.1 | additional information | enzyme synthesis is subject to catabolite repression by glucose and is suppressed under aerobic conditions | Escherichia coli | ? | - |
? | |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.1 | additional information | - |
- |
Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.1 | 7.8 | - |
in the absence of MgCl2 | Escherichia coli |
| 4.3.1.1 | 8.8 | - |
native enzyme in the presence of MgCl2 | Escherichia coli |
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