Activating Compound | Comment | Organism | Structure |
---|---|---|---|
N-acetylglucosamine 6-phosphate | - |
Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | comparison of KM of unmodified and N-terminal modified enzyme | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A759 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
side-chain modification | enzyme is chemically transaminated, modifying its N-terminal methionine residue to a 2-oxo-4-(methylthio)butyryl group, the transamination markedly reduces the affinity of the enzyme for its allosteric activator N-acetylglucosamine 6-phosphate, in contrast with the unmodified enzyme, which behaves as a typical allosteric K-enzyme, the modified enzyme becomes a mixed K-V allosteric protein, borohydride reduction to obtain the corresponding enzyme with a terminal hydroxy group, this enzyme shows significant recovery of the catalytic catalytic activity and its allosteric activation pattern, becomes similar to that found for the unmodified enzyme | Escherichia coli |
side-chain modification | the modification by diethyl dicarbonate results in complete inactivation of enzyme | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glucosamine 6-phosphate + H2O | - |
Escherichia coli | D-fructose 6-phosphate + NH3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | comparison of kcat of unmodified and N-terminal modified enzyme | Escherichia coli |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
effect of pH on homotropic co-operativity in the native and modified deaminases | Escherichia coli |