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Results 1 - 10 of 32 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 2.1.1.107Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.107D227A full activity 485091
Show all pathways known for 2.1.1.107Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.107D248A no transmethylase activity 485091
Show all pathways known for 2.1.1.107Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.107D303A full activity 485091
Show all pathways known for 2.1.1.107Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.107D47N binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1 662638
Show all pathways known for 2.1.1.107Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.107E114Q increase in the root mean square deviations of the uroporphyrinogen III substrate in respect to the wild-type 758359
Show all pathways known for 2.1.1.107Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.107E114Q the mutant shows strongly reduced activity compared to the wild type enzyme 719948
Show all pathways known for 2.1.1.107Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.107F106A considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity 662638
Show all pathways known for 2.1.1.107Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.107G12A 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
Show all pathways known for 2.1.1.107Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.107G189K 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
Show all pathways known for 2.1.1.107Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.107G189K the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme 719948
Results 1 - 10 of 32 > >>