Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311

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

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

We have isolated, purified and characterized arylmalonate decarboxylase (AMDase; EC 4.1.1.76). 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
Volume104
Issue number4
DOIs
Publication statusPublished - 2007 Oct

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Achromobacter
Purification
Enzymes
Alcaligenes
Gene encoding
Molecular mass
Nucleotides
Genes
Amino acids
Soil
malonate decarboxylase
Proteins
Soils
Amino Acids

Keywords

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

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering

Cite this

Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311. / Miyamoto, Kenji; Yatake, Yoshito; Tamura, Keisuke; Terao, Yosuke; Ohta, Hiromichi.

In: Journal of Bioscience and Bioengineering, Vol. 104, No. 4, 10.2007, p. 263-267.

Research output: Contribution to journalArticle

Miyamoto, Kenji ; Yatake, Yoshito ; Tamura, Keisuke ; Terao, Yosuke ; Ohta, Hiromichi. / Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311. In: Journal of Bioscience and Bioengineering. 2007 ; Vol. 104, No. 4. pp. 263-267.
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