EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.22 | A104L |
ubstitution introduced to fill a cavity in the E state and sterically prevent repacking of the core into the inactive Eomega state. Mutant A104L does not show hysteresis or negative cooperativity, binds UDP-xylose with lower affinity and the inhibition is no longer cooperative |
760597 |
| 1.1.1.22 | A136M |
mutant does not exhibit substrate cooperativity. The inhibitor affinity of A136M is reduced 14fold and does not exhibit hysteresis. Substitution disrupts NAD+-induced negative cooperativity |
760583 |
| 1.1.1.22 | A222Q/S233G |
is a dimer in solution |
695880 |
| 1.1.1.22 | A222Q/S233G |
mutation does not affect expression, stability, and secondary structure. Mutant protein is a dimer and catalytic active, with increased Km values for substrates |
687474 |
| 1.1.1.22 | A44V |
mutation is the genetic cause of a developmental epileptic encephalopathy in a consanguineous Palestinian family with three affected siblings. The A44V variant is also found in two additional families from Puerto Rico and from Spain |
761985 |
| 1.1.1.22 | C260A |
mutation of the essential Cys residue. The C260A mutant and wild-type are then co-expressed in vivo via a single-crossover homologous recombination method. The resulting strain produces an amide derivative of hyaluronan |
761284 |
| 1.1.1.22 | C260A |
no oxidation of UDP-glucose to glucuronic acid, but capable of both reducing the aldehyde intermediate and oxidizing the hydrated form of the aldehyde intermediate, protein is expressed in inclusion bodies |
655477 |
| 1.1.1.22 | C276A |
is a hexamer-dimer mixture |
695880 |
| 1.1.1.22 | C276A |
site-directed mutagenesis, strong decrease in specific activity |
685143 |
| 1.1.1.22 | C276E |
activity is not measurable at pH 8.7, 22°C |
667848 |
