Improved enantioselectivity of a lipase by rational protein engineering.
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Structural Redesign of Lipase B from Candida antarctica by Circular Permutation and Incremental TruncationRational design of enantioselective enzymes requires considerations of entropyModeling structure and flexibility of Candida antarctica lipase B in organic solvents.Structure-based substrate screening for an enzyme.Analysis of the conformational stability and activity of Candida antarctica lipase B in organic solvents: insight from molecular dynamics and quantum mechanics/simulations.How a single-point mutation in horseradish peroxidase markedly enhances enantioselectivity.Controlling the enantioselectivity of enzymes by directed evolution: practical and theoretical ramifications.Protein engineering of α/β-hydrolase fold enzymes.Substrate entropy in enzyme enantioselectivity: an experimental and molecular modeling study of a lipase.Open and closed states of Candida antarctica lipase B: protonation and the mechanism of interfacial activation.Alleviation of proteolytic sensitivity to enhance recombinant lipase production in Escherichia coli.A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases.Learning from directed evolution: theoretical investigations into cooperative mutations in lipase enantioselectivity.The effect of imidazolium cations on the structure and activity of the Candida antarctica Lipase B enzyme in ionic liquids.The relationship between enhanced enzyme activity and structural dynamics in ionic liquids: a combined computational and experimental study.Compensation of the enantioselectivity-activity trade-off in the directed evolution of an esterase from Rhodobacter sphaeroides by site-directed saturation mutagenesis.Creating space for large secondary alcohols by rational redesign of Candida antarctica lipase B.Effect of folding factors in rescuing unstable heterologous lipase B to enhance its overexpression in the periplasm of Escherichia coli.Rational and Semirational Protein Design.Controlling enantioselectivity of esterase in asymmetric hydrolysis of aryl prochiral diesters by introducing aromatic interactions.Engineering of Yarrowia lipolytica lipase Lip8p by circular permutation to alter substrate and temperature characteristics.Polycationic amino acid tags enhance soluble expression of Candida antarctica lipase B in recombinant Escherichia coli
P2860
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P2860
Improved enantioselectivity of a lipase by rational protein engineering.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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2001年学术文章
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name
Improved enantioselectivity of a lipase by rational protein engineering.
@en
Improved enantioselectivity of a lipase by rational protein engineering.
@nl
type
label
Improved enantioselectivity of a lipase by rational protein engineering.
@en
Improved enantioselectivity of a lipase by rational protein engineering.
@nl
prefLabel
Improved enantioselectivity of a lipase by rational protein engineering.
@en
Improved enantioselectivity of a lipase by rational protein engineering.
@nl
P2093
P1433
P1476
Improved enantioselectivity of a lipase by rational protein engineering
@en
P2093
D Rotticci
J C Rotticci-Mulder
P304
P356
10.1002/1439-7633(20011001)2:10<766::AID-CBIC766>3.0.CO;2-K
P577
2001-10-01T00:00:00Z