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Literature summary for 4.1.1.4 extracted from
- Origin of the pKa shift of the catalytic lysine in acetoacetate decarboxylase (2010), FEBS Lett., 584, 3464-3468.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E76Q | the optimum pH value for the enzymatic activity remains essentially unchanged in the E76Q mutation | Clostridium acetobutylicum |
| E76Q | the optimum pH value for the enzymatic activity remains essentially unchanged in the E76Q mutation | Chromobacterium violaceum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Chromobacterium violaceum | Q7NSA6 | - |
- |
| Clostridium acetobutylicum | P23670 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Acetoacetate | - |
Clostridium acetobutylicum | Acetone + CO2 | - |
? |  |
| Acetoacetate | - |
Chromobacterium violaceum | Acetone + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homododecamer | - |
Clostridium acetobutylicum |
| homododecamer | - |
Chromobacterium violaceum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AADase | - |
Clostridium acetobutylicum |
| AADase | - |
Chromobacterium violaceum |
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Release 2023.1 (January 2023)
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