EC Number   |
Protein Variants |
Reference |
|---|
  1.5.1.54 | A177V |
mutation mimicks human polymorphism A222V. Mutation does not affect kcat or the Km values but alters FAD binding |
762001 |
| 1.5.1.54 | D120A |
midpoint potential of the mutant increases, the mutant exhibits a 1.2- to 1.5fold faster reduction rate than the wild-type enzyme. Catalytic efficiency (kcat/Km) in the 5-10-methylentetrahydrofolate oxidative half-reaction is significantly decreased |
760566 |
| 1.5.1.54 | D120K |
midpoint potential of the mutant increases, the mutant exhibits a 1.2- to 1.5fold faster reduction rate than the wild-type enzyme. Catalytic efficiency (kcat/Km) in the 5-10-methylentetrahydrofolate oxidative half-reaction is significantly decreased |
760566 |
| 1.5.1.54 | D120N |
midpoint potential of the mutant increases, the mutant exhibits a 1.2- to 1.5fold faster reduction rate than the wild-type enzyme. Catalytic efficiency (kcat/Km) in the 5-10-methylentetrahydrofolate oxidative half-reaction is significantly decreased |
760566 |
| 1.5.1.54 | D120N |
mutant is reduced by NADH 30% more rapidly than the wild-type enzyme |
760563 |
| 1.5.1.54 | D120S |
midpoint potential of the mutant increases, the mutant exhibits a 1.2- to 1.5fold faster reduction rate than the wild-type enzyme. Catalytic efficiency (kcat/Km) in the 5-10-methylentetrahydrofolate oxidative half-reaction is significantly decreased |
760566 |
| 1.5.1.54 | D120V |
midpoint potential of the mutant increases, the mutant exhibits a 1.2- to 1.5fold faster reduction rate than the wild-type enzyme. Catalytic efficiency (kcat/Km) in the 5-10-methylentetrahydrofolate oxidative half-reaction is significantly decreased |
760566 |
| 1.5.1.54 | E28Q |
mutant is unable to catalyze the reduction of 5,10-methylentetrahydrofolate and is inactive in the physiological oxidoreductase reaction. The mutant is able to bind methyltetrahydrofolate, but reduction of the FAD cofactor is not observed |
760563 |
| 1.5.1.54 | F223A |
mutation impairs NADH and 5,10-methylentetrahydrofolate binding each 40fold yet slows catalysis of both half-reactions less than 2fold |
760569 |
| 1.5.1.54 | F223L |
affinity for 5,10-methylentetrahydrofolate is unaffected by the mutation, the variant catalyzes the oxidative half-reaction 3fold faster than the wild-type enzyme |
760569 |
