Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311

Kenji Miyamoto, Yoshito Yatake, Keisuke Tamura, Yosuke Terao, Hiromichi Ohta

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


We have isolated, purified and characterized arylmalonate decarboxylase (AMDase; EC This is an unique enzyme that gives optically pure arylpropionates from the corresponding arylmalonates. Recently, we have screened similar enzyme producers from soil samples and succeeded in isolating Achromobacter sp. KU1311. The gene encoding the enzyme was cloned and sequenced. The AMDase gene consists of 720 nucleotides, which specifies a 240 amino acid protein with a relative molecular mass of 24,735. This enzyme was purified and its characteristics were compared with those of the hitherto known enzyme from Alcaligenes bronchisepticus KU1201.

Original languageEnglish
Pages (from-to)263-267
Number of pages5
JournalJournal of Bioscience and Bioengineering
Issue number4
Publication statusPublished - 2007 Oct


  • Achromobacter sp.
  • arylmalonate decarboxylase
  • asymmetric decarboxylation
  • purification

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


Dive into the research topics of 'Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311'. Together they form a unique fingerprint.

Cite this