Crystallization and preliminary X-ray analysis of L - Azetidine-2- carboxylate hydrolase from Pseudomonas sp. strain A2C

Mayuko Toyoda; Keiji Jitsumori; Bunzo Mikami; Lawrence P. Wackett; Tatsuo Kurihara; Nobuyoshi Esaki

doi:10.1107/S1744309110017045

Crystallization and preliminary X-ray analysis of L - Azetidine-2- carboxylate hydrolase from Pseudomonas sp. strain A2C

Mayuko Toyoda, Keiji Jitsumori, Bunzo Mikami, Lawrence P. Wackett, Tatsuo Kurihara, Nobuyoshi Esaki

Synthetic Biology and Biotechnology Division

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Abstract

L-Azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C catalyzes a ring-opening reaction that detoxifies L-azetidine-2-carboxylate, an analogue of L-proline. Recombinant L-azetidine-2-carboxylate hydrolase was overexpressed, purified and crystallized using polyethylene glycol and magnesium acetate as precipitants. The needle-shaped crystal belonged to space group P2₁, with unit-cell parameters a = 35.6, b = 63.6, c = 54.7 Å, β = 105.5°. The crystal diffracted to a resolution of 1.38 Å. The calculated V_M value was 2.2 Å³ Da^-1, suggesting that the crystal contains one enzyme subunit in the asymmetric unit.

Original language	English (US)
Pages (from-to)	801-804
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	66
Issue number	7
DOIs	https://doi.org/10.1107/S1744309110017045
State	Published - 2010

Keywords

L-azetidine-2-carboxylate hydrolase
Pseudomonas sp. strain A2C

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Crystallization and preliminary X-ray analysis of L - Azetidine-2- carboxylate hydrolase from Pseudomonas sp. strain A2C. / Toyoda, Mayuko; Jitsumori, Keiji; Mikami, Bunzo et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 66, No. 7, 2010, p. 801-804.

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

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abstract = "L-Azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C catalyzes a ring-opening reaction that detoxifies L-azetidine-2-carboxylate, an analogue of L-proline. Recombinant L-azetidine-2-carboxylate hydrolase was overexpressed, purified and crystallized using polyethylene glycol and magnesium acetate as precipitants. The needle-shaped crystal belonged to space group P21, with unit-cell parameters a = 35.6, b = 63.6, c = 54.7 {\AA}, β = 105.5°. The crystal diffracted to a resolution of 1.38 {\AA}. The calculated VM value was 2.2 {\AA}3 Da-1, suggesting that the crystal contains one enzyme subunit in the asymmetric unit.",

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AU - Toyoda, Mayuko

AU - Jitsumori, Keiji

AU - Mikami, Bunzo

AU - Wackett, Lawrence P.

AU - Kurihara, Tatsuo

AU - Esaki, Nobuyoshi

PY - 2010

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AB - L-Azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C catalyzes a ring-opening reaction that detoxifies L-azetidine-2-carboxylate, an analogue of L-proline. Recombinant L-azetidine-2-carboxylate hydrolase was overexpressed, purified and crystallized using polyethylene glycol and magnesium acetate as precipitants. The needle-shaped crystal belonged to space group P21, with unit-cell parameters a = 35.6, b = 63.6, c = 54.7 Å, β = 105.5°. The crystal diffracted to a resolution of 1.38 Å. The calculated VM value was 2.2 Å3 Da-1, suggesting that the crystal contains one enzyme subunit in the asymmetric unit.

KW - L-azetidine-2-carboxylate hydrolase

KW - Pseudomonas sp. strain A2C

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Crystallization and preliminary X-ray analysis of L - Azetidine-2- carboxylate hydrolase from Pseudomonas sp. strain A2C

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Keywords

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