EC Number   |
Protein Variants |
Reference |
|---|
    5.4.99.2 | E392A |
site-directed mutagenesis, kcat is reduced 12fold compared to the wild-type enzyme. The mutant shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate |
727036 |
| 5.4.99.2 | E392D |
site-directed mutagenesis, kcat is reduced 330fold compared to the wild-type enzyme. The mutant shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate |
727036 |
| 5.4.99.2 | E392Q |
site-directed mutagenesis, kcat is reduced 16fold compared to the wild-type enzyme. The mutant shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate |
727036 |
| 5.4.99.2 | G623R |
six missense mutations, producing the amino acid changes G94V, Y231N, R369H, G623R, H678R and G717V are detected in L-methylmalonyl-CoA mutase cDNA of patients suffering from the mut-form of methylmalonic acidemia resulting from defective adenosylcobalamin binding. The mutations increase the Km for adenosylcobalamin by 40fold to 900fold, while the values for maximal velocity varies from 0.2% to nearly 100% of that of the wild-type protein |
3518 |
| 5.4.99.2 | G717V |
six missense mutations, producing the amino acid changes G94V, Y231N, R369H, G623R, H678R and G717V are detected in L-methylmalonyl-CoA mutase cDNA of patients suffering from the mut-form of methylmalonic acidemia resulting from defective adenosylcobalamin binding. The mutations increase the Km for adenosylcobalamin by 40fold to 900fold, while the values for maximal velocity varies from 0.2% to nearly 100% of that of the wild-type protein |
3518 |
| 5.4.99.2 | G94V |
six missense mutations, producing the amino acid changes G94V, Y231N, R369H, G623R, H678R and G717V are detected in L-methylmalonyl-CoA mutase cDNA of patients suffering from the mut-form of methylmalonic acidemia resulting from defective adenosylcobalamin binding. The mutations increase the Km for adenosylcobalamin by 40fold to 900fold, while the values for maximal velocity varies from 0.2% to nearly 100% of that of the wild-type protein |
3518 |
| 5.4.99.2 | H224Q |
lower turnover than wild-type enzyme |
650005 |
| 5.4.99.2 | H244A |
lower turnover than wild-type enzyme |
650005 |
| 5.4.99.2 | H610A |
weakened affinity to the cofactor and much lower turnover than wild-type enzyme |
652252 |
| 5.4.99.2 | H610N |
weakened affinity to the cofactor and much lower turnover than wild-type enzyme |
652252 |
