EC Number   |
Protein Variants |
Reference |
|---|
    6.2.1.5 | A103D |
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome |
745500 |
| 6.2.1.5 | A307V |
the mutation is associated with succinyl-CoA ligase (ATP-forming) or succinyl-CoA synthetase (ADP-forming) deficiency |
745783 |
| 6.2.1.5 | C123ALPHAA |
lower catalytic efficiency compared to the wild type enzyme |
671076 |
| 6.2.1.5 | C123ALPHAS |
lower catalytic efficiency compared to the wild type enzyme |
671076 |
| 6.2.1.5 | C123ALPHAT |
lower catalytic efficiency compared to the wild type enzyme |
671076 |
| 6.2.1.5 | C123ALPHAV |
lower catalytic efficiency compared to the wild type enzyme |
671076 |
| 6.2.1.5 | C325E |
Cys325Glu mutant is 83% as active as the wild type enzyme. The mutant enzyme is refractory to chemical modification by CoA disulfide-S,S-dioxide and methyl methane thiosulfonate. It is less reactive with NEM |
812 |
| 6.2.1.5 | E197betaA |
mutant enzyme with very low activity. The mutant protein is crystallized in the same space group as the wild-type enzyme. Crystals of the mutant enzyme grew as plates rather than as cubes which are the usual crystal habit for the wild-type enzyme |
650157 |
| 6.2.1.5 | E197betaD |
the Km-values and turnover numbers are comparable to those of the wild-type enzyme |
650157 |
| 6.2.1.5 | E197betaQ |
the KM-value for each substrate is comparable to that of the wild-type enzyme, except for GTP, whose Km-value is reduced by a factor of 20. 3000fold decrease in turnover number for reaction with ATP, 7000fold decrease in turnover-number when using GTP |
650157 |
