Enhancement of the latent 3-isopropylmalate dehydrogenase activity of promiscuous homoisocitrate dehydrogenase by directed evolution

Biochemical Journal

Volumn 431, Issue 3, 2010, Pages 401-410

  Suzuki, Yumewo ^a,c   Asada, Kuniko ^a,d   Miyazaki, Junichi ^a,e   Tomita, Takeo ^a   Kuzuyama, Tomohisa ^a   Nishiyama, Makoto ^a,b  

^a UNIVERSITY OF TOKYO   (Japan)

^b RIKEN SPring 8 Center ^*  (Japan)

^c DSP Food and Chemical Co   (Japan)

^d MITSUBISHI CHEMICAL CORPORATION   (Japan)

^e JAPAN AGENCY FOR MARINE EARTH SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

Directed evolution; DNA shuffling; Leucine biosynthesis; Lysine biosynthesis; Substrate specificity

Indexed keywords

BINDING ENERGY; BINDING SITES; BIOCHEMISTRY; BIOLOGY; BIOSYNTHESIS; CRYSTAL STRUCTURE; DNA; ENZYME ACTIVITY; ESCHERICHIA COLI; SUBSTRATES;

DIRECTED EVOLUTION; DNA SHUFFLING; LEUCINE BIOSYNTHESIS; LYSINE BIOSYNTHESIS; SUBSTRATE SPECIFICITY;

AMINO ACIDS;

3 ISOPROPYLMALATE DEHYDROGENASE; HOMOISOCITRATE DEHYDROGENASE; ISOCITRATE DEHYDROGENASE; ISOCITRIC ACID; UNCLASSIFIED DRUG; ALCOHOL DEHYDROGENASE;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; DNA SHUFFLING; ENZYME ACTIVITY; ESCHERICHIA COLI; HEAT TOLERANCE; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; SCREENING; SITE DIRECTED MUTAGENESIS; TEMPERATURE SENSITIVITY; THERMUS THERMOPHILUS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MUTATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI; THERMUS THERMOPHILUS;

3-ISOPROPYLMALATE DEHYDROGENASE; ALCOHOL OXIDOREDUCTASES; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MUTATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY; THERMUS THERMOPHILUS;

EID: 78049232833     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101246     Document Type: Article

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