Protein Variants | Comment | Organism |
---|---|---|
K115C | mutant enzymes K115C and K115Q are catalytically inactive at pH 5.95. Mutant enzymes K116C, K116N and K116R have reduced but significant activities | Clostridium acetobutylicum |
K115Q | mutant enzymes K115C and K115Q are catalytically inactive at pH 5.95. Mutant enzymes K116C, K116N and K116R have reduced but significant activities | Clostridium acetobutylicum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
8.2 | - |
acetoacetate | wild-type enzyme | Clostridium acetobutylicum | |
8.4 | - |
acetoacetate | mutant enzyme K116C | Clostridium acetobutylicum | |
10 | - |
acetoacetate | mutant enzyme K116N | Clostridium acetobutylicum | |
14.7 | - |
acetoacetate | mutant enzyme K116R | Clostridium acetobutylicum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium acetobutylicum | - |
wild-type and mutant enzymes K115C, K115Q, K116C, K116N and K116R | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
acetoacetate = acetone + CO2 | mechanism | Clostridium acetobutylicum | |
acetoacetate = acetone + CO2 | Schiff base intermediate | Clostridium acetobutylicum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Acetoacetate | - |
Clostridium acetobutylicum | Acetone + CO2 | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
30 | - |
acetoacetate | mutant enzyme K116N | Clostridium acetobutylicum | |
38 | - |
acetoacetate | mutant enzyme K116C | Clostridium acetobutylicum | |
302 | - |
acetoacetate | mutant enzyme K116R | Clostridium acetobutylicum | |
1560 | - |
acetoacetate | wild-type enzyme | Clostridium acetobutylicum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
wild-type enzyme | Clostridium acetobutylicum |