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Results 1 - 10 of 17 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 5.3.2.1E16A kinetics similar to wild-type 678575
Display the word mapDisplay the reaction diagram Show all sequences 5.3.2.1E52Q mutation in alpha-subunit, 1.6fold increase in ratio of kcat to Km value -, 678327
Display the word mapDisplay the reaction diagram Show all sequences 5.3.2.1K32A 15fold decrease in Ki-value for the competitive inhibitor, (E)-2-fluoro-p-hydroxycinnamate compared to wild-type enzyme, turnover number for enol-phenylpyruvate is 9% of that for the wild-type enzyme, turnover number for enol-(p-hydroxyphenyl)pyruvate is 11% of that for the wild-type enzyme, the ratio of turnover number and Km-value for enol-phenylpyruvate is 8% of that for the wild-type enzyme, the ratio of turnover number and KM-value for enol(p-hydroxyphenyl)pyruvate is 16% of the value for the wild-type enzyme 649881
Display the word mapDisplay the reaction diagram Show all sequences 5.3.2.1K32R modest decrease in the stereoselectivity of the reaction and in the binding affinity of the competitive inhibitor, (E)-2-fluoro-p-hydroxycinnamate, turnover number for enol-phenylpyruvate is 47% of that for the wild-type enzyme, turnover number for enol-(p-hydroxyphenyl)pyruvate is 110% of that for the wild-type enzyme, the ratio of turnover number and Km-value for enol-phenylpyruvate or enol(p-hydroxyphenyl)pyruvate is about 70% of the value for the wild-type enzyme 649881
Display the word mapDisplay the reaction diagram Show all sequences 5.3.2.1more modification of Pro1, e.g. via isothiocyanate inhibitors, alters the tertiary, but not the secondary or quaternary, structure of the trimer without affecting its thermodynamic stability, overview 702357
Display the word mapDisplay the reaction diagram Show all sequences 5.3.2.1N97A the ratio of turnover number to Km-value for enol-phenylpyruvate is 21.3fold higher than that of the wild-type enzyme, the ratio of turnover number to Km-value for enol-(p-hydroxyphenyl)pyruvate is 1.5fold lower than that of the wild-type enzyme, 5fold increase in Ki-value for (E)-2-fluoro-p-hydroxycinnamate compared to the wild-type enzyme 650013
Display the word mapDisplay the reaction diagram Show all sequences 5.3.2.1P1(A)M2 insertion abolishes activity 649900
Display the word mapDisplay the reaction diagram Show all sequences 5.3.2.1P1A for phenylenolpyruvate, the P1A mutant shows a 41fold decrease in kcat and a 14fold decrease in Km, resulting in an about 3fold decrease in kcat/Km. For (4-hydroxyphenyl)enolpyruvate, the P1A mutant shows a 16fold decrease in kcat, whereas the Km is not significantly affected, resulting in a 16fold decrease in kcat/Km. The P1A mutant has no detectable dehalogenase activity toward cis-3-chloroacrylate and trans-3-chloroacrylate, and no detectable activity toward 2-oxo-3-pentynoate (at pH 7.3) -, 714241
Display the word mapDisplay the reaction diagram Show all sequences 5.3.2.1P1A mutation in beta-subunit, 8fold decrease in ratio of kcat to Km value -, 678327
Display the word mapDisplay the reaction diagram Show all sequences 5.3.2.1P1A the ratio of turnover number to Km-value for enol-phenylpyruvate is 232fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for enol-(p-hydroxyphenyl)pyruvate is 114fold lower than that of the wild-type enzyme 650013
Results 1 - 10 of 17 > >>