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Results 1 - 10 of 12 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.29S90C 30fold increase in Km-value for tRNATyr and 4fold increase in Km-value for guanine 644934
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.29D89E about 50% of the activity of the histidine-tagged wild-type enzyme 644933
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.29S90A activity of the mutant enzyme is to low to determine Vmax and Km-value 644934
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.29Y106F crystallises similarly to the wild-type 703226
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.29D264N is inactive and incapable of forming the covalent intermediate, while maintaining the ability to bind noncovalently to RNA 702263
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.29D89A less than 1% of the activity of the histidine-tagged wild-type enzyme 644933
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.29D89C less than 1% of the activity of the histidine-tagged wild-type enzyme 644933
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.29D89N less than 1% of the activity of the histidine-tagged wild-type enzyme 644933
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.29S90F mutant enzyme has no detectable solubility and reduced solubility 644934
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.29K52M reduced turnover value. At a concentration of protein of 0.01 mM appears almost exclusively as a homodimer as the wild-type, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident 705164
Results 1 - 10 of 12 > >>