EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.5.1.47 | in complex with substrate analog citrate, at 1.33 A resolution. The C1-carboxylate of citrate is bound at the carboxylate position of O-acetylserine, whereas the C6-carboxylate adopts two conformations. Modeling of the unnatural substrate 5-thio-2-nitrobenzoate into the structure | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.5.1.47 | Q140E | inactive | Escherichia coli |
2.5.1.47 | Q240A | ratio kcat to Km value is 0.4% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy | Escherichia coli |
2.5.1.47 | R210A | ratio kcat to Km value is 2% of wild-type | Escherichia coli |
2.5.1.47 | T68A | ratio kcat to Km value is 0.1% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy | Escherichia coli |
2.5.1.47 | T68S | ratio kcat to Km value is 55% of wild-type | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.47 | 0.6 | - |
O-acetyl-L-serine | mutant T68S, 37°C | Escherichia coli | |
2.5.1.47 | 0.7 | - |
O-acetyl-L-serine | wild-type, 37°C | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.47 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.47 | O-acetyl-L-serine + 5-thio-2-nitrobenzoate | - |
Escherichia coli | ? + acetate | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.47 | 11 | - |
O-acetyl-L-serine | mutant T68S, 37°C | Escherichia coli | |
2.5.1.47 | 24 | - |
O-acetyl-L-serine | wild-type, 37°C | Escherichia coli |