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