Activity improvement of UDP-galactose-4-epimerase for tagatose substrates by 3D structure-based combinatorial mutagenesis

Journal of Molecular Catalysis B: Enzymatic

Volumn 84, Issue , 2012, Pages 35-39

  Kim, Hye Jung ^a   Kang, Sueng Yeun ^a   Choi, Joon Ho ^b   Kim, Pil ^a  

^a The Catholic University of Korea   (South Korea)

^b Wonkwang University   (South Korea)

Author keywords

3D structure docking model; Enzyme evolution; Monosaccharide 4 epimerase; UDP galactose 4 epimerase

Indexed keywords

3D STRUCTURE; COFACTOR BINDING; DOCKING MODELS; DOUBLE MUTANTS; HIGH ACTIVITY; KINETIC STUDY; MONOSACCHARIDE 4-EPIMERASE; RANDOM MUTATION; SINGLE MUTATION; STRUCTURE-BASED; SUBSTRATE-BINDING; TAGATOSE; UDP-GALACTOSE-4-EPIMERASE; WILD TYPES; WILD-TYPE ENZYMES;

CLONING; DOCKING; ENZYMES; GLUCOSE; KINETIC PARAMETERS; SUBSTRATES;

THREE DIMENSIONAL;

TAGATOSE; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

BIOTRANSFORMATION; COMBINATORIAL LIBRARY; COMBINATORIAL MUTAGENESIS; CONFERENCE PAPER; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; EPIMERIZATION; ESCHERICHIA COLI; MOLECULAR DOCKING; MUTAGENESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; SATURATION MUTAGENESIS;

EID: 84866347141     PISSN: 13811177     EISSN: 18733158     Source Type: Journal    
DOI: 10.1016/j.molcatb.2012.04.020     Document Type: Conference Paper

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