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

Xiuzhen Gao | Zendy; Fang Huang | Zendy; Jinhui Feng | Zendy; Xi Chen | Zendy; Hailing Zhang | Zendy; Zhixiang Wang | Zendy; Qiaqing Wu | Zendy; Dunming Zhu | Zendy

Open Access

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

Author(s) -

Xiuzhen Gao,

Fang Huang,

Jinhui Feng,

Xi Chen,

Hailing Zhang,

Zhixiang Wang,

Qiaqing Wu,

Dunming Zhu

Publication year - 2013

Publication title -

applied and environmental microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.552

H-Index - 324

eISSN - 1070-6291

pISSN - 0099-2240

DOI - 10.1128/aem.01049-13

Subject(s) - saturated mutagenesis , mutant , mutagenesis , site directed mutagenesis , protein engineering , biochemistry , amino acid , dehydrogenase , enzyme , chemistry , substrate (aquarium) , phenylalanine , saturation (graph theory) , biology , stereochemistry , ecology , gene , mathematics , combinatorics

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.

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