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Article

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

Acta crystallographica. Section F, Structural biology and crystallization communications - 1 Jun 2010

Shibata Naoki, Tamagaki Hiroko, Ohtsuki Shungo, Hieda Naoki, Akita Keita, Komori Hirofumi, Shomura Yasuhito, Terawaki Shin-ichi, Toraya Tetsuo, Yasuoka Noritake, Higuchi Yoshiki

Abstract excerpt

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 w...

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Identifiers

PMID: 20516606
DOI: 10.1107/S1744309110014478
PMCID: PMC2882776

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-20516606-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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