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

Yoshito Yatake, Kenji Miyamoto, Hiromichi Ohta

研究成果: Article査読

12 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)793-799
ページ数7
ジャーナルApplied Microbiology and Biotechnology
78
5
DOI
出版ステータスPublished - 2008 4

ASJC Scopus subject areas

  • バイオテクノロジー
  • 応用微生物学とバイオテクノロジー

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