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Literature summary extracted from
- Characterization of three types of aspartase activated by site-directed mutagenesis, limited proteolysis, and acetylation (1993), J. Biochem., 114, 735-739.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.1 | alpha-methyl-DL-aspartate | activates wild-type enzyme, mutant C-terminal-truncated and acetylated enzyme | Escherichia coli |  |
| 4.3.1.1 | L-aspartate | activates the fumarate-amination reaction | Escherichia coli | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.1.1 | Escherichia coli | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.3.1.1 | L-aspartate = fumarate + NH3 | mechanism | Escherichia coli |
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 | additional information | - |
- |
Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.1.1 | L-aspartate | r | Escherichia coli | fumarate + NH3 | - |
? | |
| 4.3.1.1 | L-aspartate | natural substrate | Escherichia coli | fumarate + NH3 | - |
? | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.1 | additional information | - |
- |
Escherichia coli |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.1 | additional information | - |
- |
Escherichia coli |
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Release 2023.1 (January 2023)
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