title: Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates.
abstract: Catalytic activity and enantioselectivity of lipase toward poor substrates bearing bulky substituents on both sides have been dramatically improved by rational design; the E value for a poor substrate was increased from 5 (wild-type enzyme) to >200 (I287F/I290A double mutant) with an acceleration of the reaction rate.
authors.affiliation: Division of Chemistry and Biochemistry, Graduate School of Natural Science and Technology, Okayama University, Tsushima, Okayama 700-8530, Japan. ema@cc.okayama-u.ac.jp
authors.forename: Tadashi
authors.initials: T
authors.lastname: Ema
authors.forename: Shusuke
authors.initials: S
authors.lastname: Kamata
authors.forename: Masahiro
authors.initials: M
authors.lastname: Takeda
authors.forename: Yasuko
authors.initials: Y
authors.lastname: Nakano
authors.forename: Takashi
authors.initials: T
authors.lastname: Sakai
mesh_terms: D016956:Burkholderia cepacia / Q000201:enzymology*; D008049:Lipase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D011994:Recombinant Proteins; D008049:Lipase