EC Number | Cloned (Comment) | Organism |
---|---|---|
3.11.1.1 | expression of wild-type and mutant enzymes in Escherichia coli JM109 | Bacillus cereus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.11.1.1 | K121R/K146R/K192R | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Bacillus cereus |
3.11.1.1 | K183A | site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment | Bacillus cereus |
3.11.1.1 | K183L | site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment | Bacillus cereus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.11.1.1 | 2,4-Dinitrophenylacetate | loss of activity due to acetylation of Ls53 with the inert compound, pH profile of inactivation | Bacillus cereus | |
3.11.1.1 | Trypsin | degradation | Bacillus cereus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.11.1.1 | additional information | - |
additional information | kinetics | Bacillus cereus | |
3.11.1.1 | 0.033 | - |
phosphonoacetaldehyde | wild-type enzyme, pH 7.5, 25°C | Bacillus cereus | |
3.11.1.1 | 0.056 | - |
phosphonoacetaldehyde | triple mutant K121R/K146R/K192R, pH 7.5, 25°C | Bacillus cereus | |
3.11.1.1 | 0.193 | - |
phosphonoacetaldehyde | mutant K183A, pH 7.5, 25°C | Bacillus cereus | |
3.11.1.1 | 0.77 | - |
phosphonoacetaldehyde | mutant K183L, pH 7.5, 25°C | Bacillus cereus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.11.1.1 | Mg2+ | required for catalysis | Bacillus cereus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.11.1.1 | Bacillus cereus | O31156 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate | mechanism, active site conformation during catalysis, Lys53 is involved | Bacillus cereus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.11.1.1 | phosphonoacetaldehyde + H2O | i.e. Pald, cleavage via Schiff base intermediate formed with Lys53, bound substrate stabilizes the closed conformation of the active site, thus facilitating catalysis | Bacillus cereus | acetaldehyde + phosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.11.1.1 | 2-phosphonoacetaldehyde phosphonohydrolase | - |
Bacillus cereus |
3.11.1.1 | phosphonatase | - |
Bacillus cereus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.11.1.1 | 0.012 | - |
phosphonoacetaldehyde | mutant K183A, pH 7.5, 25°C | Bacillus cereus | |
3.11.1.1 | 0.046 | - |
phosphonoacetaldehyde | mutant K183L, pH 7.5, 25°C | Bacillus cereus | |
3.11.1.1 | 1.28 | - |
phosphonoacetaldehyde | triple mutant K121R/K146R/K192R, pH 7.5, 25°C | Bacillus cereus | |
3.11.1.1 | 6.08 | - |
phosphonoacetaldehyde | triple mutant K121R/K146R/K192R, pH 7.5, 25°C | Bacillus cereus | |
3.11.1.1 | 15 | - |
phosphonoacetaldehyde | wild-type enzyme, pH 7.5, 25°C | Bacillus cereus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.11.1.1 | additional information | - |
additional information | inhibition kinetics | Bacillus cereus |