EC Number |
Protein Variants |
Reference |
---|
2.3.3.14 | D123N |
mutant |
704648 |
2.3.3.14 | E155A |
mutant enzyme exhibits 1000fold lower activity than wild-type enzyme. Activity of E155A can be partially rescued by formate |
685263 |
2.3.3.14 | E155Q |
mutant enzyme exhibits 1000fold lower activity than wild-type enzyme. The kcat for E155Q decreases at high pH, similar to the wild-type enzyme, but is pH independent at low pH |
685263 |
2.3.3.14 | E167A |
mutant, reveals the contribution of this residue to substrate binding and catalysis |
704600 |
2.3.3.14 | E167Q |
mutant, reveals the contribution of this residue to substrate binding and catalysis |
704600 |
2.3.3.14 | E222Q |
mutant |
704648 |
2.3.3.14 | E74A |
mutant, reveals the contribution of this residue to substrate binding and catalysis |
704600 |
2.3.3.14 | E74Q |
mutant, reveals the contribution of this residue to substrate binding and catalysis |
704600 |
2.3.3.14 | H103A |
mutant, reveals the contribution of this residue to substrate binding and catalysis |
704600 |
2.3.3.14 | H309A |
inactive mutant enzyme. Slight increase in activity is observed for H309A in the presence of 300 mM imidazole, which is still 1000fold lower than that of wild type |
685263 |