EC Number   |
Inhibitors |
Structure |
|---|
   4.1.2.22 | (NH4)2SO4 |
- |
   |
| 4.1.2.22 | ATP |
phosphoenolpyruvate and oxaloacetic acid share the same or have overlapping allosteric binding sites, while ATP binds at a separate site |
|
| 4.1.2.22 | glyoxylate |
7.2% residual activity at 8 mM |
|
| 4.1.2.22 | hydroxylamine |
- |
|
| 4.1.2.22 | Iodosobenzoate |
- |
|
| 4.1.2.22 | more |
the enzyme is unaffected by the presence of ATP, AMP, pyruvate, and acetate |
|
| 4.1.2.22 | oxaloacetic acid |
phosphoenolpyruvate and oxaloacetic acid share the same or have overlapping allosteric binding sites, while ATP binds at a separate site. AMP and phosphoenolpyruvate/oxaloacetic acid operate independently, with AMP activating Xfp2 and phosphoenolpyruvate/oxaloacetic acid inhibiting the activated enzyme |
|
| 4.1.2.22 | oxaloacetic acid |
about 30% residual activity at 15 mM |
|
| 4.1.2.22 | p-hydroxymercuribenzoate |
- |
|
| 4.1.2.22 | phosphoenolpyruvate |
phosphoenolpyruvate and oxaloacetic acid share the same or have overlapping allosteric binding sites, while ATP binds at a separate site. AMP and phosphoenolpyruvate/oxaloacetic acid operate independently, with AMP activating Xfp2 and phosphoenolpyruvate/oxaloacetic acid inhibiting the activated enzyme |
|
