Crystallization (Comment) | Organism |
---|---|
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 |
Protein Variants | Comment | Organism |
---|---|---|
Q140E | inactive | Escherichia coli |
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 |
R210A | ratio kcat to Km value is 2% of wild-type | Escherichia coli |
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 |
T68S | ratio kcat to Km value is 55% of wild-type | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.6 | - |
O-acetyl-L-serine | mutant T68S, 37°C | Escherichia coli | |
0.7 | - |
O-acetyl-L-serine | wild-type, 37°C | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
O-acetyl-L-serine + 5-thio-2-nitrobenzoate | - |
Escherichia coli | ? + acetate | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
11 | - |
O-acetyl-L-serine | mutant T68S, 37°C | Escherichia coli | |
24 | - |
O-acetyl-L-serine | wild-type, 37°C | Escherichia coli |