EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    4.2.3.1 | DL-3-chloroalanine |
beta-elimination |
Escherichia coli |
pyruvate + NH3 + HCl |
- |
ir |
| 4.2.3.1 | DL-vinylglycine + H2O |
- |
Escherichia coli |
L-threonine |
- |
ir |
| 4.2.3.1 | L-allo-threonine + H2O |
beta-elimination |
Escherichia coli |
2-oxobutyrate + NH3 |
- |
ir |
| 4.2.3.1 | L-serine |
beta-elimination |
Escherichia coli |
pyruvate + NH3 |
- |
ir |
| 4.2.3.1 | L-vinylglycine + phosphate + H2O |
in the presence of phosphate, L-threonine is formed with kcat and reaction specificity comparable with those when O-phospho-L-homoserine is used as the substrate. In the absence of phosphate or when sulfate is used in place of phosphate, only the side reaction product, alpha-ketobutyrate, is formed. Compared with the more acidic sulfate ion, the phosphate ion decreases the energy levels of the transition states of the addition of water at the Cbeta of the PLP-alpha-aminocrotonate aldimine and the transaldimination to form L-threonine. Threonine synthase is in the closed form, when the substrate and the intermediates are bound to the enzyme |
Thermus thermophilus |
L-threonine + phosphate |
- |
? |
| 4.2.3.1 | L-vinylglycine + phosphate + H2O |
in the presence of phosphate, L-threonine is formed with kcat and reaction specificity comparable with those when O-phospho-L-homoserine is used as the substrate. In the absence of phosphate or when sulfate is used in place of phosphate, only the side reaction product, alpha-ketobutyrate, is formed. Compared with the more acidic sulfate ion, the phosphate ion decreases the energy levels of the transition states of the addition of water at the Cbeta of the PLP-alpha-aminocrotonate aldimine and the transaldimination to form L-threonine. Threonine synthase is in the closed form, when the substrate and the intermediates are bound to the enzyme |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 |
L-threonine + phosphate |
- |
? |
| 4.2.3.1 | more |
- |
Bacillus subtilis |
? |
- |
? |
| 4.2.3.1 | more |
half-transamination reactions |
Escherichia coli |
? |
- |
? |
| 4.2.3.1 | O-phospho-L-homoserine |
studies on regulatory properties |
Escherichia coli |
? |
- |
? |
| 4.2.3.1 | O-phospho-L-homoserine |
involved in allocation of phosphohomoserine between cystathione and threonine pathways |
Beta vulgaris |
? |
- |
? |
