Crystallization and preliminary X-ray diffraction experiments of arylmalonate decarboxylase from Alcaligenes bronchisepticus

Masayoshi Nakasako, Rika Obata, Ryosuke Okubo, Shyuichi Nakayama, Kenji Miyamoto, Hiromichi Ohta

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Arylmalonate decarboxylase catalyses the enantioselective decarboxylation of α-aryl-α-methylmalonates to produce optically pure α-arylpropionates. The enzyme was crystallized with ammonium sulfate under alkaline pH conditions with the aim of understanding the mechanism of the enantioselective reaction. X-ray diffraction data collected to a resolution of 3.0 Å at cryogenic temperature showed that the crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 83.13, b = 99.62, c = 139.64 Å. This suggested that the asymmetric unit would contain between four and six molecules. Small-angle X-ray scattering revealed that the enzyme exists as a monomer in solution. Thus, the assembly of molecules in the asymmetric unit was likely to have been induced during the crystallization process.

Original languageEnglish
Pages (from-to)610-613
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number7
DOIs
Publication statusPublished - 2008

Fingerprint

Alcaligenes
Crystallization
X-Ray Diffraction
enzymes
crystallization
X ray diffraction
decarboxylation
ammonium sulfates
Decarboxylation
Molecules
Ammonium Sulfate
Enzymes
cryogenic temperature
X ray scattering
diffraction
Cryogenics
molecules
x rays
monomers
assembly

Keywords

  • Alcaligenes bronchisepticus
  • Arylmalonate decarboxylase
  • Enantioselectivity

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

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title = "Crystallization and preliminary X-ray diffraction experiments of arylmalonate decarboxylase from Alcaligenes bronchisepticus",
abstract = "Arylmalonate decarboxylase catalyses the enantioselective decarboxylation of α-aryl-α-methylmalonates to produce optically pure α-arylpropionates. The enzyme was crystallized with ammonium sulfate under alkaline pH conditions with the aim of understanding the mechanism of the enantioselective reaction. X-ray diffraction data collected to a resolution of 3.0 {\AA} at cryogenic temperature showed that the crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 83.13, b = 99.62, c = 139.64 {\AA}. This suggested that the asymmetric unit would contain between four and six molecules. Small-angle X-ray scattering revealed that the enzyme exists as a monomer in solution. Thus, the assembly of molecules in the asymmetric unit was likely to have been induced during the crystallization process.",
keywords = "Alcaligenes bronchisepticus, Arylmalonate decarboxylase, Enantioselectivity",
author = "Masayoshi Nakasako and Rika Obata and Ryosuke Okubo and Shyuichi Nakayama and Kenji Miyamoto and Hiromichi Ohta",
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T1 - Crystallization and preliminary X-ray diffraction experiments of arylmalonate decarboxylase from Alcaligenes bronchisepticus

AU - Nakasako, Masayoshi

AU - Obata, Rika

AU - Okubo, Ryosuke

AU - Nakayama, Shyuichi

AU - Miyamoto, Kenji

AU - Ohta, Hiromichi

PY - 2008

Y1 - 2008

N2 - Arylmalonate decarboxylase catalyses the enantioselective decarboxylation of α-aryl-α-methylmalonates to produce optically pure α-arylpropionates. The enzyme was crystallized with ammonium sulfate under alkaline pH conditions with the aim of understanding the mechanism of the enantioselective reaction. X-ray diffraction data collected to a resolution of 3.0 Å at cryogenic temperature showed that the crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 83.13, b = 99.62, c = 139.64 Å. This suggested that the asymmetric unit would contain between four and six molecules. Small-angle X-ray scattering revealed that the enzyme exists as a monomer in solution. Thus, the assembly of molecules in the asymmetric unit was likely to have been induced during the crystallization process.

AB - Arylmalonate decarboxylase catalyses the enantioselective decarboxylation of α-aryl-α-methylmalonates to produce optically pure α-arylpropionates. The enzyme was crystallized with ammonium sulfate under alkaline pH conditions with the aim of understanding the mechanism of the enantioselective reaction. X-ray diffraction data collected to a resolution of 3.0 Å at cryogenic temperature showed that the crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 83.13, b = 99.62, c = 139.64 Å. This suggested that the asymmetric unit would contain between four and six molecules. Small-angle X-ray scattering revealed that the enzyme exists as a monomer in solution. Thus, the assembly of molecules in the asymmetric unit was likely to have been induced during the crystallization process.

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