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Engineering the meso-Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum by Site Saturation Mutagenesis for d-Phenylalanine Synthesis

机译:通过位点饱和诱变工程化嗜热共生细菌的内消旋二氨基庚二酸酯脱氢酶,用于合成d-苯丙氨酸

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In order to enlarge the substrate binding pocket of the meso -diaminopimelate dehydrogenase from Symbiobacterium thermophilum to accommodate larger 2-keto acids, four amino acid residues (Phe146, Thr171, Arg181, and His227) were targeted for site saturation mutagenesis. Among all mutants, the single mutant H227V had a specific activity of 2.39 ± 0.06 U · mg~(?1), which was 35.1-fold enhancement over the wild-type enzyme.
机译:为了扩大嗜热链球菌的内消旋二氨基庚二酸脱氢酶的底物结合口袋以容纳更大的2-酮酸,将四个氨基酸残基(Phe146,Thr171,Arg181和His227)用于位点饱和诱变。在所有突变体中,单个突变体H227V的比活为2.39±0.06 U·mg〜(?1),比野生型酶高35.1倍。

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