Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311

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

doi:10.1263/jbb.104.263

Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311

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

Department of Biosciences and Informatics

Research output: Contribution to journal › Article › peer-review

13 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 language	English
Pages (from-to)	263-267
Number of pages	5
Journal	Journal of Bioscience and Bioengineering
Volume	104
Issue number	4
DOIs	https://doi.org/10.1263/jbb.104.263
Publication status	Published - 2007 Oct

Keywords

Achromobacter sp.
arylmalonate decarboxylase
asymmetric decarboxylation
purification

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1263/jbb.104.263

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title = "Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311",

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.",

keywords = "Achromobacter sp., arylmalonate decarboxylase, asymmetric decarboxylation, purification",

author = "Kenji Miyamoto and Yoshito Yatake and Keisuke Tamura and Yosuke Terao and Hiromichi Ohta",

note = "Funding Information: This work was partly supported by the Ministry of Education, Culture, Sports, Science and Technology, Grant-in-Aid for “Science and Technology Program on Molecules, Supra-Molecules, and Supra-Structured Materials” of the Academic frontier promotional project. The financial support from Takeda Science Foundation is also gratefully acknowledged.",

year = "2007",

month = oct,

doi = "10.1263/jbb.104.263",

language = "English",

volume = "104",

pages = "263--267",

journal = "Journal of Bioscience and Bioengineering",

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T1 - Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311

AU - Miyamoto, Kenji

AU - Yatake, Yoshito

AU - Tamura, Keisuke

AU - Terao, Yosuke

AU - Ohta, Hiromichi

N1 - Funding Information: This work was partly supported by the Ministry of Education, Culture, Sports, Science and Technology, Grant-in-Aid for “Science and Technology Program on Molecules, Supra-Molecules, and Supra-Structured Materials” of the Academic frontier promotional project. The financial support from Takeda Science Foundation is also gratefully acknowledged.

PY - 2007/10

Y1 - 2007/10

N2 - 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.

AB - 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.

KW - Achromobacter sp.

KW - arylmalonate decarboxylase

KW - asymmetric decarboxylation

KW - purification

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ER -

Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311

Abstract

Keywords

ASJC Scopus subject areas

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