Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
E347F | mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type | Escherichia coli |
E442A | mutation increases the K0.5 value of Thr and n(H) value, comparing to those of the wild-type enzyme. IC50 (Ile) is decreased compared to wild-type | Escherichia coli |
F352A | mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type | Escherichia coli |
F352A/I460F | double mutant is more resistant to Ile inhibition than any single site mutant. Double mutations retains more than 85% activity even at 10 mM Ile | Escherichia coli |
F352A/R362F | mutant shows both higher activity and stronger resistance to Ile inhibition compared to wild-type mice. Overexpression of mutant in Escherichia coli JW3591 significantly increases the production of ketobutyrate and Ile in comparison to the reference strains overexpressing wild-type | Escherichia coli |
G350E | mutation increases the K0.5 value of Thr and n(H) value, comparing to those of the wild-type enzyme. IC50 (Ile) is decreased compared to wild-type | Escherichia coli |
G445E | mutation G445E increased the K0.5 value of Thr without change of n(H) value compared to wild-type. IC50 (Ile) is slightly increased compared to wild-type | Escherichia coli |
I460F | mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type | Escherichia coli |
I460F/R362F | double mutant is more resistant to Ile inhibition than any single site mutant. Double mutations retains more than 85% activity even at 10 mM Ile | Escherichia coli |
R362F | mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type | Escherichia coli |
Y369L | mutant shows an 91fold increased IC50 (Ile) value compared to wild-type | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ile | inhibition of isoleucine can be reversed by valine | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
Threonine deaminase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.009 | - |
pH 7.5, 30°C, mutant E442A | Escherichia coli | Ile | |
0.037 | - |
pH 7.5, 30°C, mutant G350E | Escherichia coli | Ile | |
0.067 | - |
pH 7.5, 30°C, wild-type | Escherichia coli | Ile | |
0.162 | - |
pH 7.5, 30°C, mutant G445E | Escherichia coli | Ile | |
2.32 | - |
pH 7.5, 30°C, mutant F352A | Escherichia coli | Ile | |
2.86 | - |
pH 7.5, 30°C, mutant E347F | Escherichia coli | Ile | |
3.27 | - |
pH 7.5, 30°C, mutant I460F | Escherichia coli | Ile | |
6.99 | - |
pH 7.5, 30°C, mutant R362F | Escherichia coli | Ile |