Stereochemistry of decarboxylation of arylmalonate catalyzed by mutant enzymes

Kenji Miyamoto; Tomomi Tsutsumi; Yosuke Terao; Hiromichi Ohta

doi:10.1246/cl.2007.656

Stereochemistry of decarboxylation of arylmalonate catalyzed by mutant enzymes

Kenji Miyamoto, Tomomi Tsutsumi, Yosuke Terao, Hiromichi Ohta

Department of Biosciences and Informatics

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

The enantiotopos differentiating selectivity of the mutant arylmalonate decarboxylase (S36N/G74C/C188S), which catalyzes asymmetric decarboxylation of arylmethylmalonates to give the corresponding arylpropionates, was revealed to be the same as that of the wild type enzyme, in spite of the fact that two enzymes gave the opposite enantiomer with each other.

Original language	English
Pages (from-to)	656-657
Number of pages	2
Journal	Chemistry Letters
Volume	36
Issue number	5
DOIs	https://doi.org/10.1246/cl.2007.656
Publication status	Published - 2007 May 5

ASJC Scopus subject areas

Chemistry(all)

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10.1246/cl.2007.656

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abstract = "The enantiotopos differentiating selectivity of the mutant arylmalonate decarboxylase (S36N/G74C/C188S), which catalyzes asymmetric decarboxylation of arylmethylmalonates to give the corresponding arylpropionates, was revealed to be the same as that of the wild type enzyme, in spite of the fact that two enzymes gave the opposite enantiomer with each other.",

author = "Kenji Miyamoto and Tomomi Tsutsumi and Yosuke Terao and Hiromichi Ohta",

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AU - Miyamoto, Kenji

AU - Tsutsumi, Tomomi

AU - Terao, Yosuke

AU - Ohta, Hiromichi

PY - 2007/5/5

Y1 - 2007/5/5

N2 - The enantiotopos differentiating selectivity of the mutant arylmalonate decarboxylase (S36N/G74C/C188S), which catalyzes asymmetric decarboxylation of arylmethylmalonates to give the corresponding arylpropionates, was revealed to be the same as that of the wild type enzyme, in spite of the fact that two enzymes gave the opposite enantiomer with each other.

AB - The enantiotopos differentiating selectivity of the mutant arylmalonate decarboxylase (S36N/G74C/C188S), which catalyzes asymmetric decarboxylation of arylmethylmalonates to give the corresponding arylpropionates, was revealed to be the same as that of the wild type enzyme, in spite of the fact that two enzymes gave the opposite enantiomer with each other.

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Stereochemistry of decarboxylation of arylmalonate catalyzed by mutant enzymes

Abstract

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