Stereochemistry of decarboxylation of arylmalonate catalyzed by mutant enzymes

Kenji Miyamoto, Tomomi Tsutsumi, Yosuke Terao, Hiromichi Ohta

Research output: Contribution to journalArticle

4 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 languageEnglish
Pages (from-to)656-657
Number of pages2
JournalChemistry Letters
Volume36
Issue number5
DOIs
Publication statusPublished - 2007 May 5

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Stereochemistry
Enantiomers
Enzymes
Decarboxylation
malonate decarboxylase

ASJC Scopus subject areas

  • Chemistry(all)

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Stereochemistry of decarboxylation of arylmalonate catalyzed by mutant enzymes. / Miyamoto, Kenji; Tsutsumi, Tomomi; Terao, Yosuke; Ohta, Hiromichi.

In: Chemistry Letters, Vol. 36, No. 5, 05.05.2007, p. 656-657.

Research output: Contribution to journalArticle

Miyamoto, Kenji ; Tsutsumi, Tomomi ; Terao, Yosuke ; Ohta, Hiromichi. / Stereochemistry of decarboxylation of arylmalonate catalyzed by mutant enzymes. In: Chemistry Letters. 2007 ; Vol. 36, No. 5. pp. 656-657.
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