EC Number   |
Protein Variants |
Reference |
|---|
    5.4.3.5 | C700S |
site-directed mutagenesis, the beta-subunit mutant shows similar kinetics and activity as the wild-type enzyme |
748182 |
| 5.4.3.5 | D627A |
site-directed mutagenesis, the beta-subunit mutant shows similar kinetics and slightly reduced activity compared to the wild-type enzyme |
748182 |
| 5.4.3.5 | E338A |
site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 670fold and catalytic efficiency 220fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate |
-, 727036 |
| 5.4.3.5 | E338A |
site-directed mutagenesis, the beta-subunit mutant shows a reduced turnover number compared to wild-type enzyme, while the Km value is similar |
747738 |
| 5.4.3.5 | E338A |
site-directed mutagenesis, the beta-subunit mutant shows altered kinetics and highly reduced activity compared to the wild-type enzyme |
748182 |
| 5.4.3.5 | E338D |
site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 380fold and catalytic efficiency 60fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows n detectable adenosylcobalamin homolysis upon binding of the physiological substrate |
-, 727036 |
| 5.4.3.5 | E338D |
site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 380fold and catalytic efficiency 60fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate |
-, 727036 |
| 5.4.3.5 | E338D |
site-directed mutagenesis, the beta-subunit mutant shows a reduced turnover number compared to wild-type enzyme, while the Km value is similar |
747738 |
| 5.4.3.5 | E338Q |
site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 90fold and catalytic efficiency 20fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate |
-, 727036 |
| 5.4.3.5 | E338Q |
site-directed mutagenesis, the beta-subunit mutant shows a reduced turnover number compared to wild-type enzyme, while the Km value is similar |
747738 |
