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In order to enlarge the substrate binding pocket of themeso -diaminopimelate dehydrogenase fromSymbiobacterium 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.

applied and environmental microbiology

Engineering the <i>meso</i> -Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum by Site Saturation Mutagenesis for <scp>d</scp> -Phenylalanine Synthesis

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