Asymmetric decarboxylation of α-hydroxy- and α-amino-α-phenylmalonate catalyzed by arylmalonate decarboxylase from Alcaligenes bronchisepticus

Keisuke Tamura, Yosuke Terao, Kenji Miyamoto, Hiromichi Ohta

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Arylmalonate decarboxylase (EC 4.1.1.76, from Alcaligenes bronchisepticus KU 1201) is an enzyme that catalyzes asymmetric decarboxylation of arylmalonate. The enzyme accepts as substrates compounds that have a sterically small hydrophobic α-substituent, such as H, F, and methyl. To widen the applicability of this enzyme and to obtain information on the interaction between the enzyme and substrates, we tried the reaction of compounds with a hydrophilic substituent. Although the relative reactivities were lower compared to that of phenylmalonate, α-hydroxy- and α-aminophenylmalonate were decarboxylated to give optically active monobasic acids.

Original languageEnglish
Pages (from-to)253-257
Number of pages5
JournalBiocatalysis and Biotransformation
Volume26
Issue number4
DOIs
Publication statusPublished - 2008 Jul 1

Keywords

  • Arylmalonate decarboxylase
  • Enzymatic decarboxylation
  • α-aminomalonate
  • α-hydroxymalonate

ASJC Scopus subject areas

  • Biotechnology
  • Catalysis
  • Biochemistry

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