EC Number   |
Protein Variants |
Reference  |
|---|
    5.1.2.2 | N197A |
Kcat for (R)-mandelate reduced 30fold, Kcat for (S)-mandelate reduced 179fold relative to wild-type |
285167 |
| 5.1.2.2 | D270N |
structure of D270N with (S)-atrolactate bound in the active site reveals no geometric alterations when compared to the structure of the wild type enzyme complexed with (S)-atrolactate, with the exception that the side chain of His297 is tilted and displaced about 0.5A away from Asn270 and towards the (S)-atrolactate. The turnover number for both (R)-mandelate and (S)-mandelate are reduced 10000fold |
285178 |
| 5.1.2.2 | H297N |
H297N has no detectable mandelate racemase activity. However, H297N catalyzes the stereospecific elimination of Br- from racemic p-(bromomethyl)mandelate to give p-(methyl)benzoylformate in 45% yield at a rate equal to that measured for wild type enzyme |
285186 |
| 5.1.2.2 | H297N |
H297N, which is inactive as a racemase catalyzes the stereospecific exchange of the alpha-proton of S- but not R-mandelate with solvent D2O at a rate that is 30% of that of the wild type enzyme |
285189 |
| 5.1.2.2 | K166E |
K166R retains low level of racemase activity. K166R mutant catalyzes the elimination of Br- from only the (R)-enantiomer of (R,S)-p-(bromomethyl)mandelate |
285192 |
| 5.1.2.2 | E317Q |
E317Q with 3400fold reduced turnover number for (R)-mandelate and 29000fold reduced turnover number for (S)-mandelate. E317Q mutant enzyme does not catalyze detectable elimination of Br- from either enantiomer of p-(bromomethyl)mandelate. E317Q mutant enzyme is irreversibly inactivated by racemic alpha-phenylglycidate at a rate comparable to that measured for wild type enzyme |
285194 |
| 5.1.2.2 | N197A |
turnover number is reduced 30fold for (R)-mandelate and 179fold for (S)-mandelate relative to wild-type enzyme. The ratio of turnover number to Km-value is reduced 208fold for (R)-mandelate and 556fold for (S)-mandelate, 3.5fold reduction in affinity for the substrate analogue (R)-atrolactate, but 51fold and 18fold reduction in affinity for alpha-hydroxybenzylphosphonate and benzohydroxamate, respectively |
285195 |
| 5.1.2.2 | N197A |
slight activating effect of sucrose on mutant enzyme efficiency. In presewnce of polymeric viscosogens poly(ethylene glycol) and Ficoll, no effect on turnover number or the ratio of turnover number and Km-value for the wild-type enzyme is observed |
650147 |
| 5.1.2.2 | F52W |
compared to wild-type enzyme the catalytic preference of the mutant enzyme is reversed and catalytic efficiency is reduced. Mutant enzyme exhibits higher affinity for (R)-mandelate than for (S)-mandelate, and a higher turnover number with (S)-mandelate as the substrate, relative to that with (R)-mandelate |
661212 |
| 5.1.2.2 | F52W/Y54W |
compared to wild-type enzyme the catalytic preference of the mutant enzyme is reversed and catalytic efficiency is reduced. Mutant enzyme exhibits higher affinity for (R)-mandelate than for (S)-mandelate, and a higher turnover number with (S)-mandelate as the substrate, relative to that with (R)-mandelate |
661212 |
