EC Number |
Protein Variants |
Reference |
---|
5.1.2.2 | A25V |
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate |
690962 |
5.1.2.2 | A25V |
site-directed mutagenesis |
726974 |
5.1.2.2 | A25V |
variation of the hydrophobic loop, decrease in catalytic efficiency |
690962 |
5.1.2.2 | C92S/C264S/K166C |
site-directed mutagenesis |
727042 |
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 | 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 | 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 |
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 |