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Results 1 - 10 of 72 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 5.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.2.2A25V 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
Show all pathways known for 5.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.2.2A25V site-directed mutagenesis 726974
Show all pathways known for 5.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.2.2A25V variation of the hydrophobic loop, decrease in catalytic efficiency 690962
Show all pathways known for 5.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.2.2C92S/C264S/K166C site-directed mutagenesis 727042
Show all pathways known for 5.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.2.2D270N 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
Show all pathways known for 5.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.2.2E317Q 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
Show all pathways known for 5.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.2.2F52W 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
Show all pathways known for 5.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.2.2F52W/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
Show all pathways known for 5.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.2.2H297N 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
Show all pathways known for 5.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.2.2H297N 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
Results 1 - 10 of 72 > >>