EC Number |
Protein Variants |
Reference |
---|
4.1.1.7 | A460G |
mutant exhibits a higher Km value compared to the wild type enzyme |
691794 |
4.1.1.7 | A460I |
activity with pyruvate is higher than wild-type activity, activity with 2-oxobutanoic acid is 2.3fold higher than wild-type activity, activity with 2-oxopentanoic acid is 1.1fold lower than wild-type activity, activity with 2-oxohexanoic acid is 3.3fold higher than wild-type activity, activity with 3-methyl-2-oxobutanoic acid is 1.3fold higher than wild-type activity, activity with 3-methyl-2-oxopentanoic acid is 1.1fold lower than wild-type activity, activity with 2-oxo-4-methylpentanoic acid is 1.3fold higher than wild-type activity, activity with 4,4-dimethyl-2-oxopentanoic acid is identical to wild-type activity, activity with 2-oxo-4-methylhexanoic acid is 2.2fold higher than wild-type activity, activity with benzoylformate is 22.5fold lower than wild-type activity, activity with 2-oxo-3-phenylpropanoic acid is identical to wild-type activity, activity with 2-oxo-4-phenylbutanoic acid is 1.8fold higher than wild-type activity, activity with 2-oxo-5-phenylpentanoic acid is identical to wild-type activity. The ratio of turnover number to KM-value for 2-oxo-4-methylpentanoic acid is 10fold higher than the wild-type value, the ratio of turnover number to KM-value for 2-oxo-4-methylhexanoic acid is 1.13fold higher than the wild-type value, the ratio of turnover number to KM-value for benzoylformate is 5.4fold lower than the wild-type value, the ratio of turnover number to KM-value for 2-oxohexanoic acid is 14.1fold higher than the wild-type value, the ratio of turnover number to KM-value for 2-oxopentanoic acid is 4.6fold higher than the wild-type value. Mutation has no effect on the range of products obtained by carboligation of acetaldehyde and benzaldehyde, the yield of the product 2-hydroxypropiophenone an decreases about 3fold and the enantioselectivity of acetoin and 2-hydroxypropiophenone is altered |
666806 |
4.1.1.7 | A460I |
for this variant the highest amounts of (S)-2-hydroxypropiophenone-product can be detected at low benzaldehyde concentrations and slightly acidic conditions at pH 6.5 |
702796 |
4.1.1.7 | A460I |
site-directed mutagenesis, the mutant enzymes is an excellent 2-ketohexanoate decarboxylase |
727483 |
4.1.1.7 | A460I |
strongly decreased activity |
679209 |
4.1.1.7 | A460I |
the mutant exhibits an increased (R)-2-hydroxypropiophenone selectivity |
715697 |
4.1.1.7 | A460I/F464I |
activity with pyruvate is higher than wild-type activity, activity with 2-oxobutanoic acid is 1.8fold lower than wild-type activity, activity with 2-oxopentanoic acid is 9.2fold lower than wild-type value, activity with 2-oxohexanoic acid is 3.3fold lower than wild-type activity, activity with 3-methyl-2-oxobutanoic acid is 1.5fold lower than wild-type activity, activity with 3-methyl-2-oxopentanoic acid is 1.2fold lower than wild-type activity, activity with 2-oxo-4-methylpentanoic acid is 1.5fold lower than wild-type activity, activity with 4,4-dimethyl-2-oxopentanoic acid is 10fold lower than wild-type activity, activity with 2-oxo-4-methylhexanoic acid is 1.1fold lower than wild-type activity, activity with benzoylformate is 64.3fold lower than wild-type activity, no activity with 2-oxo-3-phenylpropanoic acid, activity with 2-oxo-4-phenylbutanoic acid is 1.3fold lower than wild-type activity, activity with 2-oxo-5-phenylpentanoic acid is fold higher than wild-type activity. the ratio of turnover number to KM-value for benzoylformate is 88.7fold lower than the wild-type value |
666806 |
4.1.1.7 | A460I/F464I |
for this variant the highest amounts of (S)-2-hydroxypropiophenone-product can be detected at low benzaldehyde concentrations and slightly acidic conditions at pH 6.5 |
702796 |
4.1.1.7 | A460I/F464I |
strongly decreased activity |
679209 |
4.1.1.7 | A460I/F464I |
the mutant exhibits an increased (R)-2-hydroxypropiophenone selectivity |
715697 |