Any feedback?
Literature summary extracted from
- Origin of the pKa shift of the catalytic lysine in acetoacetate decarboxylase (2010), FEBS Lett., 584, 3464-3468.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.1.1.4 | E76Q | the optimum pH value for the enzymatic activity remains essentially unchanged in the E76Q mutation | Clostridium acetobutylicum |
| 4.1.1.4 | E76Q | the optimum pH value for the enzymatic activity remains essentially unchanged in the E76Q mutation | Chromobacterium violaceum |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.4 | Chromobacterium violaceum | Q7NSA6 | - |
- |
| 4.1.1.4 | Clostridium acetobutylicum | P23670 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.4 | Acetoacetate | - |
Clostridium acetobutylicum | Acetone + CO2 | - |
? |  |
| 4.1.1.4 | Acetoacetate | - |
Chromobacterium violaceum | Acetone + CO2 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.1.1.4 | homododecamer | - |
Clostridium acetobutylicum |
| 4.1.1.4 | homododecamer | - |
Chromobacterium violaceum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.1.4 | AADase | - |
Clostridium acetobutylicum |
| 4.1.1.4 | AADase | - |
Chromobacterium violaceum |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
