Stereochemistry of decarboxylation of arylmalonate catalyzed by mutant enzymes

Kenji Miyamoto, Tomomi Tsutsumi, Yosuke Terao, Hiromichi Ohta

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


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
Issue number5
Publication statusPublished - 2007 May 5

ASJC Scopus subject areas

  • Chemistry(all)


Dive into the research topics of 'Stereochemistry of decarboxylation of arylmalonate catalyzed by mutant enzymes'. Together they form a unique fingerprint.

Cite this