EC Number   |
Protein Variants |
Reference |
|---|
    4.2.1.11 | D257K |
the mutation has no effect on excystation |
730352 |
| 4.2.1.11 | DELTA434-435 |
mutant with decreased Glu- and Lys-plasminogen-binding activities |
651496 |
| 4.2.1.11 | deltaK433/K434 |
mutant with different oligomerization state |
666033 |
| 4.2.1.11 | E168Q |
severely depressed activity, does not catalyze hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3, alters the tautomeric state or catalyzes ionization of bound tartronate semialdehyde phosphate |
33642 |
| 4.2.1.11 | E168Q |
the Mg2+ binding site is different compared to the wild type enzyme |
650225 |
| 4.2.1.11 | E168Q |
the mutant has approximately 0.01% of the activity of native enolase. It binds 3-aminoenolpyruvate-2-phosphate, the 3-amino analogue of the product phosphoenolpyruvate and D-tartronate semialdehyde-2-phosphate, the aldehyde analogue of the substrate 2-phosphoglycerate, the latter two with affinities similar to those of the native enzyme |
33636 |
| 4.2.1.11 | E211Q |
can exchange the alpha proton of 2-phospho-D-glycerate, but cannot catalyze the complete dehydration to phosphoenolpyruvate |
650225 |
| 4.2.1.11 | E211Q |
inactive, but properly folded |
666065 |
| 4.2.1.11 | E211Q |
severely depressed activity, alters the tautomeric state or catalyzes ionization of bound tartronate semialdehyde phosphate. Glu211 participates in the second step of the reaction |
33642 |
| 4.2.1.11 | E414L |
replacement of an interface glutamate residue with a leucine does not result into dimer dissociation |
679767 |
