Unexpectedly enhanced stereoselectivity of peroxidase-catalyzed sulfoxidation in branched alcohols

Xie Yuchun, Prasanta Kumar Das, Jose M.M. Caaveiro, Alexander M. Klibanov

研究成果: ジャーナルへの寄稿記事

11 引用 (Scopus)

抄録

Lyophilized horseradish peroxidase (HRP) exhibits poor stereoselectivity in the sulfoxidation of thioanisole when the enzyme is either redissolved in water orsuspendedinorganicsolvents.However,whenHRPis co-lyophilized in the presence of lyoprotectants or ligands, its stereoselectivity, although still low in most organic solvents, increases up to 4-fold if assayed in secondary or tertiary alcohols (but not in their linear isomers). A mechanistic hypothesisis presented explaining this puzzling phenomenon on the basis of a model of the active site of the enzyme-substrate complex derived from its X-ray crystal structure by means of molecular dynamics and energy minimization.
元の言語英語
ページ(範囲)105-111
ページ数7
ジャーナルBiotechnology and Bioengineering
79
発行部数1
DOI
出版物ステータス出版済み - 2002

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Stereoselectivity
Peroxidase
Alcohols
Enzymes
Horseradish Peroxidase
Molecular Dynamics Simulation
Isomers
Organic solvents
Molecular dynamics
Catalytic Domain
Crystal structure
Ligands
X-Rays
X rays
Water
Substrates
methylphenylsulfide

これを引用

Unexpectedly enhanced stereoselectivity of peroxidase-catalyzed sulfoxidation in branched alcohols. / Yuchun, Xie; Das, Prasanta Kumar; Caaveiro, Jose M.M.; Klibanov, Alexander M.

:: Biotechnology and Bioengineering, 巻 79, 番号 1, 2002, p. 105-111.

研究成果: ジャーナルへの寄稿記事

Yuchun, Xie ; Das, Prasanta Kumar ; Caaveiro, Jose M.M. ; Klibanov, Alexander M. / Unexpectedly enhanced stereoselectivity of peroxidase-catalyzed sulfoxidation in branched alcohols. :: Biotechnology and Bioengineering. 2002 ; 巻 79, 番号 1. pp. 105-111.
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AU - Das, Prasanta Kumar

AU - Caaveiro, Jose M.M.

AU - Klibanov, Alexander M.

PY - 2002

Y1 - 2002

N2 - Lyophilized horseradish peroxidase (HRP) exhibits poor stereoselectivity in the sulfoxidation of thioanisole when the enzyme is either redissolved in water orsuspendedinorganicsolvents.However,whenHRPis co-lyophilized in the presence of lyoprotectants or ligands, its stereoselectivity, although still low in most organic solvents, increases up to 4-fold if assayed in secondary or tertiary alcohols (but not in their linear isomers). A mechanistic hypothesisis presented explaining this puzzling phenomenon on the basis of a model of the active site of the enzyme-substrate complex derived from its X-ray crystal structure by means of molecular dynamics and energy minimization.

AB - Lyophilized horseradish peroxidase (HRP) exhibits poor stereoselectivity in the sulfoxidation of thioanisole when the enzyme is either redissolved in water orsuspendedinorganicsolvents.However,whenHRPis co-lyophilized in the presence of lyoprotectants or ligands, its stereoselectivity, although still low in most organic solvents, increases up to 4-fold if assayed in secondary or tertiary alcohols (but not in their linear isomers). A mechanistic hypothesisis presented explaining this puzzling phenomenon on the basis of a model of the active site of the enzyme-substrate complex derived from its X-ray crystal structure by means of molecular dynamics and energy minimization.

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DO - 10.1002/bit.10308

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JO - Biotechnology and Bioengineering

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