EC Number |
Protein Variants |
Reference |
---|
2.1.1.107 | D227A |
full activity |
485091 |
2.1.1.107 | D248A |
no transmethylase activity |
485091 |
2.1.1.107 | D303A |
full activity |
485091 |
2.1.1.107 | D47N |
binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1 |
662638 |
2.1.1.107 | E114Q |
increase in the root mean square deviations of the uroporphyrinogen III substrate in respect to the wild-type |
758359 |
2.1.1.107 | E114Q |
the mutant shows strongly reduced activity compared to the wild type enzyme |
719948 |
2.1.1.107 | F106A |
considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity |
662638 |
2.1.1.107 | G12A |
site-directed mutagenesis of cobA abolishes the tellurite resistance of the mesophilic, heterologous host Escherichia coli and the SUMT activity in vitro. Cells overexpressing SUMT G12A show 7fold less tolerance to K2TeO3 as compared to that exhibit by cells expressing the wild-type methyltransferase |
-, 706702 |
2.1.1.107 | G189K |
increase in activity compared to wild-type. The side chain of K189 makes electrostatic interactions with the propionate side chain of ring B with an average distance of 4.0 A. The backbone of K189 makes hydrogen bonds with the propionate side chain of ring B of uroporphyrinogen III |
758359 |
2.1.1.107 | G189K |
the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme |
719948 |