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EC Number Protein Variants Commentary Reference
Show all pathways known for 3.5.3.11Display the word mapDisplay the reaction diagram Show all sequences 3.5.3.11H206A Km-value for agmatine is 2.1fold lower than the Km-value for the wild-type enzyme. kcat is 90% compared to the wild-type value 754341
Show all pathways known for 3.5.3.11Display the word mapDisplay the reaction diagram Show all sequences 3.5.3.11H394A Km-value for agmatine is 2.3fold higher than the Km-value for the wild-type enzyme. kcat ist identical to wild-type enzyme 754341
Show all pathways known for 3.5.3.11Display the word mapDisplay the reaction diagram Show all sequences 3.5.3.11H435A Km-value for agmatine is 1.5fold higher than the Km-value for the wild-type enzyme. kcat ist 70% compared to the wild-type value 754341
Show all pathways known for 3.5.3.11Display the word mapDisplay the reaction diagram Show all sequences 3.5.3.11H65A incubation of the mutant with 50 mM EDTA (pH 7.5) and subsequent dialysis to remove the chelating agent results in the loss of agmatinase activity. Even in the presence of Mn2+ only about 20% of the activity of the mutant enzyme is recovered. Km-value for agmatine is 1.44fold higher than the Km-value for the wild-type enzyme. kcat is 1.1fold higher as compared to the wild-type enzyme 754341
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