Screening, cloning, expression, and purification of an acidic arylmalonate decarboxylase from Enterobacter cloacae KU1313

Yoshito Yatake, Kenji Miyamoto, Hiromichi Ohta

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

We have already isolated, purified, and characterized arylmalonate decarboxylases (AMDase; EC. 4.1.1.76) from Alcaligenes bronchisepticus KU1201 and Achromobacter sp. KU1311. These are unique enzymes that give optically pure α-arylpropionates from the corresponding α-aryl-α- methylmalonates. Recently, we have further screened novel AMDase producers from soil samples under acidic conditions and succeeded in isolating Enterobacter cloacae KU1313. The gene encoding the enzyme was cloned by polymerase chain reaction and sequenced. The AMDase gene consists of 720 nucleotides, which specifies a 240-amino-acid protein. The recombinant enzyme was purified and shown that the pH-activity profiles were quite different from those of known AMDases.

Original languageEnglish
Pages (from-to)793-799
Number of pages7
JournalApplied Microbiology and Biotechnology
Volume78
Issue number5
DOIs
Publication statusPublished - 2008 Apr 1

Keywords

  • AMDase
  • Arylmalonate decarboxylase
  • Asymmetric decarboxylation
  • Enterobacter cloacae
  • Purification

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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