Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates.
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.
Ema
Tadashi
T
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
Kamata
Shusuke
S
Takeda
Masahiro
M
Nakano
Yasuko
Y
Sakai
Takashi
T
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
D011994:Recombinant Proteins; D008049:Lipase