Inhibitors | Comment | Organism | Structure |
---|---|---|---|
acetonylphosphonate | in presence of NH4+ | Bacillus cereus | |
fluorophosphate | competitive inhibitor | Bacillus cereus | |
malonic semialdehyde | competitive inhibitor | Bacillus cereus | |
phosphonoacetaldehyde | competitive inhibitor | Bacillus cereus | |
phosphonoethanol | competitive inhibitor | Bacillus cereus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus cereus | - |
AI-2 | - |
Bacillus cereus AI-2 | - |
AI-2 | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate | Schiff base formation with catalytic Lys and phosphonoacetaldehyde, PC-bond cleavage in the Schiff base takes place during the second partial reaction and liberation of the acetaldehyde from the resulting enamine occurs during the third partial reaction | Bacillus cereus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetonyl phosphonate + H2O | - |
Bacillus cereus | ? | - |
? | |
acetonyl phosphonate + H2O | - |
Bacillus cereus AI-2 | ? | - |
? | |
phosphonoacetylaldehyde + H2O | - |
Bacillus cereus | acetaldehyde + phosphate | - |
? | |
phosphonoacetylaldehyde + H2O | - |
Bacillus cereus AI-2 | acetaldehyde + phosphate | - |
? | |
thiophosphonoacetaldehyde + H2O | - |
Bacillus cereus | thiophosphate + acetaldehyde | - |
? | |
thiophosphonoacetaldehyde + H2O | - |
Bacillus cereus AI-2 | thiophosphate + acetaldehyde | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 8 | - |
Bacillus cereus |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
6 | - |
protonation of the active site Lys is the cause for loss of activity | Bacillus cereus |
8 | - |
deprotonation of the active site Cys may be the cause for the loss of enzyme activity | Bacillus cereus |