Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli
Ethanolamine ammonia‐lyase (EAL) catalyzes the adenosylcobalamin‐dependent conversion of ethanolamine to acetaldehyde and ammonia. The wild‐type enzyme shows a very low solubility. N‐terminal truncation of the Escherichia coli EAL β‐subunit dramatically increases the solubility of the enzyme without...
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| Published in | Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 66; no. 6; pp. 709 - 711 |
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| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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International Union of Crystallography
01.06.2010
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| Abstract | Ethanolamine ammonia‐lyase (EAL) catalyzes the adenosylcobalamin‐dependent conversion of ethanolamine to acetaldehyde and ammonia. The wild‐type enzyme shows a very low solubility. N‐terminal truncation of the Escherichia coli EAL β‐subunit dramatically increases the solubility of the enzyme without altering its catalytic properties. Two deletion mutants of the enzyme [EAL(βΔ4–30) and EAL(βΔ4–43)] have been overexpressed, purified and crystallized using the sitting‐drop vapour‐diffusion method. Crystals of EAL(βΔ4–30) and EAL(βΔ4–43) diffracted to approximately 8.0 and 2.1 Å resolution, respectively. |
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| AbstractList | Ethanolamine ammonia-lyase from
E. coli
has been overexpressed, purified and crystallized. The crystals diffracted to 2.2 Å resolution using synchrotron radiation.
Ethanolamine ammonia-lyase (EAL) catalyzes the adenosylcobalamin-dependent conversion of ethanolamine to acetaldehyde and ammonia. The wild-type enzyme shows a very low solubility. N-terminal truncation of the
Escherichia coli
EAL β-subunit dramatically increases the solubility of the enzyme without altering its catalytic properties. Two deletion mutants of the enzyme [EAL(βΔ4–30) and EAL(βΔ4–43)] have been overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method. Crystals of EAL(βΔ4–30) and EAL(βΔ4–43) diffracted to approximately 8.0 and 2.1 Å resolution, respectively. Ethanolamine ammonia‐lyase (EAL) catalyzes the adenosylcobalamin‐dependent conversion of ethanolamine to acetaldehyde and ammonia. The wild‐type enzyme shows a very low solubility. N‐terminal truncation of the Escherichia coli EAL β‐subunit dramatically increases the solubility of the enzyme without altering its catalytic properties. Two deletion mutants of the enzyme [EAL(βΔ4–30) and EAL(βΔ4–43)] have been overexpressed, purified and crystallized using the sitting‐drop vapour‐diffusion method. Crystals of EAL(βΔ4–30) and EAL(βΔ4–43) diffracted to approximately 8.0 and 2.1 Å resolution, respectively. Ethanolamine ammonia-lyase (EAL) catalyzes the adenosylcobalamin-dependent conversion of ethanolamine to acetaldehyde and ammonia. The wild-type enzyme shows a very low solubility. N-terminal truncation of the Escherichia coli EAL beta-subunit dramatically increases the solubility of the enzyme without altering its catalytic properties. Two deletion mutants of the enzyme [EAL(betaDelta4-30) and EAL(betaDelta4-43)] have been overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method. Crystals of EAL(betaDelta4-30) and EAL(betaDelta4-43) diffracted to approximately 8.0 and 2.1 A resolution, respectively. Ethanolamine ammonia-lyase (EAL) catalyzes the adenosylcobalamin-dependent conversion of ethanolamine to acetaldehyde and ammonia. The wild-type enzyme shows a very low solubility. N-terminal truncation of the Escherichia coli EAL b-subunit dramatically increases the solubility of the enzyme without altering its catalytic properties. Two deletion mutants of the enzyme [EAL(b4-30) and EAL(b4-43)] have been overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method. Crystals of EAL(b4-30) and EAL(b4-43) diffracted to approximately 8.0 and 2.1 Aa resolution, respectively. |
| Author | Tamagaki, Hiroko Komori, Hirofumi Higuchi, Yoshiki Hieda, Naoki Toraya, Tetsuo Yasuoka, Noritake Ohtsuki, Shungo Shomura, Yasuhito Shibata, Naoki Terawaki, Shin-ichi Akita, Keita |
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| Snippet | Ethanolamine ammonia‐lyase (EAL) catalyzes the adenosylcobalamin‐dependent conversion of ethanolamine to acetaldehyde and ammonia. The wild‐type enzyme shows a... Ethanolamine ammonia-lyase (EAL) catalyzes the adenosylcobalamin-dependent conversion of ethanolamine to acetaldehyde and ammonia. The wild-type enzyme shows a... Ethanolamine ammonia-lyase from E. coli has been overexpressed, purified and crystallized. The crystals diffracted to 2.2 Å resolution using synchrotron... |
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| SubjectTerms | adenosylcobalamin Crystallization Crystallization Communications Crystallography, X-Ray Escherichia coli Escherichia coli - enzymology ethanolamine ammonia-lyase Ethanolamine Ammonia-Lyase - chemistry Ethanolamine Ammonia-Lyase - genetics Gene Expression Mutation radical enzymes |
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| Title | Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli |
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