EC Number |
Protein Variants |
Reference |
---|
5.3.2.1 | E16A |
kinetics similar to wild-type |
678575 |
5.3.2.1 | E52Q |
mutation in alpha-subunit, 1.6fold increase in ratio of kcat to Km value |
-, 678327 |
5.3.2.1 | K32A |
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 |
5.3.2.1 | K32R |
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 |
5.3.2.1 | more |
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 |
5.3.2.1 | N97A |
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 |
5.3.2.1 | P1(A)M2 |
insertion abolishes activity |
649900 |
5.3.2.1 | P1A |
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 |
5.3.2.1 | P1A |
mutation in beta-subunit, 8fold decrease in ratio of kcat to Km value |
-, 678327 |
5.3.2.1 | P1A |
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 |