EC Number |
Protein Variants |
Reference |
---|
3.5.1.84 | C175S |
the mutant enzyme binds biuret but is non-catalytic. The structure of the inactive C175S mutant enzyme with substrate bound in the active site reveals that an active site cysteine (Cys175), aspartic acid (Asp36) and lysine (Lys142) form a catalytic triad, which is consistent with biochemical studies of enzyme variants |
746233 |
3.5.1.84 | F41A |
kcat/Km for buiret is 540fold lower than the wild-type value |
746233 |
3.5.1.84 | F41L |
kcat/Km for buiret is 713fold lower than the wild-type value |
746233 |
3.5.1.84 | F41W |
kcat/Km for buiret is 73fold lower than the wild-type value |
746233 |
3.5.1.84 | F41Y |
kcat/Km for buiret is 139fold lower than the wild-type value |
746233 |
3.5.1.84 | K142A |
kcat/Km for buiret is 297fold lower than the wild-type value |
746233 |
3.5.1.84 | Q215A |
kcat/Km for buiret is 419fold lower than the wild-type value |
746233 |
3.5.1.84 | Q215E |
kcat/Km for buiret is 1302fold lower than the wild-type value |
746233 |
3.5.1.84 | Q215N |
kcat/Km for buiret is 38fold lower than the wild-type value |
746233 |