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Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli.

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 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.

SUBMITTER: Shibata N

PROVIDER: S-EPMC2882776 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

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Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli.

Shibata Naoki N Tamagaki Hiroko H Ohtsuki Shungo S Hieda Naoki N Akita Keita K Komori Hirofumi H Shomura Yasuhito Y Terawaki Shin-ichi S Toraya Tetsuo T Yasuoka Noritake N Higuchi Yoshiki Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20100529 Pt 6

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-d ...[more]

PMID: 20516606

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