title: Engineering the meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum by site saturation mutagenesis for D-phenylalanine synthesis.
abstract: 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.
authors.affiliation: National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, China.
authors.forename: Xiuzhen
authors.initials: X
authors.lastname: Gao
authors.forename: Fang
authors.initials: F
authors.lastname: Huang
authors.forename: Jinhui
authors.initials: J
authors.lastname: Feng
authors.forename: Xi
authors.initials: X
authors.lastname: Chen
authors.forename: Hailing
authors.initials: H
authors.lastname: Zhang
authors.forename: Zhixiang
authors.initials: Z
authors.lastname: Wang
authors.forename: Qiaqing
authors.initials: Q
authors.lastname: Wu
authors.forename: Dunming
authors.initials: D
authors.lastname: Zhu
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000235:genetics* / Q000378:metabolism; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism; D001665:Binding Sites; D016297:Mutagenesis, Site-Directed; D010649:Phenylalanine / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D010649:Phenylalanine; D000594:Amino Acid Oxidoreductases; C020032:diaminopimelate dehydrogenase